British Library Lending Division Research Articles

Donald J. Urquhart and the integration of science with librarianship: Part 2

PurposeTo analyze the historical significance of Donald J. Urquhart, who established the National Lending Library for Science and Technology (NLL) which later was merged into the British Library Lending Division (BLLD), now called the British Library Document Supply Centre (BLDSC). His significance will be considered from the perspective of the development of science as a whole as well as library and information science in particular.Design/methodology/approachThe paper presents a short history of the probabilistic revolution, particularly as it developed in Britain in the form of biometric statistics due to Darwin's theory of evolution. It focuses on the overthrow of the normal paradigm, according to which frequency distributions in nature and society conform to the normal law of error. The paper discusses the importance of the Poisson distribution and its utilization in the construction of stochastic models that better describe reality. Here the focus is on the compound Poisson distribution in the form of the negative binomial distribution (NBD). The paper then shows how Urquhart extended the probabilistic revolution to librarianship by using the Poisson as the probabilistic model in his analyses of the 1956 external loans made by the Science Museum Library (SML) as well as in his management of the scientific and technical (sci/tech) journal collection of the NLL. Due to this, Urquhart can be considered as playing a pivotal role in the creation of bibliometrics or the statistical bases of modern library and information science. The paper relates how Urquhart's son and daughter‐in‐law, John A. and Norma C. Urquhart, completed Urquhart's probabilistic breakthrough by advancing for the first time the NBD as the model for library use in a study done at the University of Newcastle upon Tyne, connecting bibliometrics with biometrics. It concludes with a discussion of Urquhart's Law and its probabilistic implications for the use of sci/tech journals in a library system.FindingsBy being the first librarian to apply probability to the analysis of sci/tech journal use, Urquhart was instrumental in the creation of modern library and information science. His findings force a probabilistic re‐conceptualization of sci/tech journal use in a library system that has great implications for the transition of sci/tech journals from locally held paper copies to shared electronic databases.Originality/valueThis is the second part of an article describing the seminal contribution of Donald Urquhart to the development of document supply in the UK and internationally.

Donald J. Urquhart and the integration of science with librarianship: Part 1

PurposeThe purpose of this article is to analyze the historical significance of Donald J. Urquhart, who established the National Lending Library for Science and Technology (NLL) that later was merged into the British Library Lending Division (BLLD), now called the British Library Document Supply Centre (BLDSC).Design/methodology/approachThe paper presents a short history of the probabilistic revolution, particularly as it developed in the UK in the form of biometric statistics due to Darwin's theory of evolution. It focuses on the overthrow of the normal paradigm, according to which frequency distributions in nature and society conform to the normal law of error. The paper discusses the importance of the Poisson distribution and its utilization in the construction of stochastic models that better describe reality. Here the focus is on the compound Poisson distribution in the form of the negative binomial distribution (NBD). The paper then shows how Urquhart extended the probabilistic revolution to librarianship by using the Poisson as the probabilistic model in his analyses of the 1956 external loans made by the Science Museum Library (SML) as well as in his management of the scientific and technical (sci/tech) journal collection of the NLL. Thanks to this, Urquhart can be considered as playing a pivotal role in the creation of bibliometrics or the statistical bases of modern library and information science. The paper relates how Urquhart's son and daughter‐in‐law, John A. and Norma C. Urquhart, completed Urquhart's probabilistic breakthrough by advancing for the first time the NBD as the model for library use in a study executed at the University of Newcastle upon Tyne, connecting bibliometrics with biometrics. It concludes with a discussion of Urquhart's Law and its probabilistic implications for the use of sci/tech journals in a library system.FindingsBy being the first librarian to apply probability to the analysis of sci/tech journal use, Urquhart was instrumental in the creation of modern library and information science. His findings force a probabilistic re‐conceptualization of sci/tech journal use in a library system that has great implications for the transition of sci/tech journals from locally held paper copies to shared electronic databases.Originality/valueUrquhart's significance is considered from the perspective of the development of science as a whole as well as library and information science in particular.

Urquhart's and Garfield's Laws: The British controversy over their validity

AbstractThe British controversy over the validity of Urquhart's and Garfield's Laws during the 1970s constitutes an important episode in the formulation of the probability structure of human knowledge. This controversy took place within the historical context of the convergence of two scientific revolutions—the bibliometric and the biometric—that had been launched in Britain. The preceding decades had witnessed major breakthroughs in understanding the probability distributions underlying the use of human knowledge. Two of the most important of these breakthroughs were the laws posited by Donald J. Urquhart and Eugene Garfield, who played major roles in establishing the institutional bases of the bibliometric revolution. For his part, Urquhart began his realization of S. C. Bradford's concept of a national science library by analyzing the borrowing of journals on interlibrary loan from the Science Museum Library in 1956. He found that 10% of the journals accounted for 80% of the loans and formulated Urquhart's Law, by which the interlibrary use of a journal is a measure of its total use. This law underlay the operations of the National Lending Library for Science and Technology (NLLST), which Urquhart founded. The NLLST became the British Library Lending Division (BLLD) and ultimately the British Library Document Supply Centre (BLDSC). In contrast, Garfield did a study of 1969 journal citations as part of the process of creating the Science Citation Index (SCI), formulating his Law of Concentration, by which the bulk of the information needs in science can be satisfied by a relatively small, multidisciplinary core of journals. This law became the operational principle of the Institute for Scientific Information created by Garfield. A study at the BLLD under Urquhart's successor, Maurice B. Line, found low correlations of NLLST use with SCI citations, and publication of this study started a major controversy, during which both laws were called into question. The study was based on the faulty use of the Spearman rank‐correlation coefficient, and the controversy over it was instrumental in causing B. C. Brookes to investigate bibliometric laws as probabilistic phenomena and begin to link the bibliometric with the biometric revolution. This paper concludes with a resolution of the controversy by means of a statistical technique that incorporates Brookes' criticism of the Spearman rank‐correlation method and demonstrates the mutual supportiveness of the two laws.

Isolation, properties and amino acid sequences of a phospholipase A2 and its homologue without activity from the venom of a sea snake, Laticauda colubrina, from the Solomon Islands.

A phospholipase A2, Laticauda colubrina phospholipase A2 II (LcPLA-II), and a phospholipase A2 homologue, Laticauda colubrina phospholipase A2 homologue I (LcPLH-I), were isolated from the venom of the yellow-lipped sea snake, Laticauda colubrina, from the Solomon Islands. LcPLA-II showed phospholipase A2 activity towards egg-yolk phosphatidylcholine (24 mumol/min per mg at optimal conditions at 37 degrees C) and lethal potency (LD50 45 micrograms/kg body wt. intravenously in mice). Both of the activities were lost by treatment with p-bromophenacyl bromide. LcPLH-I showed neither phospholipase A2 activity nor lethal potency at a dose of 4.5 mg/kg body wt. in mice. It was not modified by the treatment with p-bromophenacyl bromide. LcPLA-II and LcPLH-I bound Ca2+ at a 1:1 molar ratio with KCa values of 105 microM and 44 microM at pH 8.0 respectively. Elucidation of the amino acid sequences of these two proteins showed that each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. The two sequences are different from each other at 22 residues and highly homologous to those from other sources. The essential histidine residue for the phospholipase A2 activity at position 48 is replaced by an asparagine residue in the homologue LcPLH-I. Details of the separation of the peptides obtained by proteinase digestions of LcPLA-II and LcPLA-I and the determination of their amino acid sequences are given in Supplementary Publication SUP 50145 (14 pages), which has been deposited at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1988) 249, 5.

Characterization and amino acid sequence of a fatty acid-binding protein from human heart.

The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.

Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus.

The pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus comprises a structural core, composed of 60 dihydrolipoamide acetyltransferase (E2p) subunits, which binds multiple copies of pyruvate decarboxylase (E1p) and dihydrolipoamide dehydrogenase (E3) subunits. After limited proteolysis with chymotrypsin, the N-terminal lipoyl domain of E2p was excised, purified and sequenced. The residual complex, which remained assembled, was then digested with trypsin under mild conditions. This treatment promoted complete disassembly of the complex and the various components were separated by gel filtration and h.p.l.c. A folded fragment of E2p containing about 50 amino acid residues was identified as being responsible for binding the E3 subunits, although, unlike the corresponding region of the E2p or E2o chains of the pyruvate dehydrogenase or 2-oxoglutarate dehydrogenase complexes from Escherichia coli, the fragment also bound E1p molecules. Further peptide purification and sequence analysis allowed the determination of the first 211 amino acid residues of the B. stearothermophilus E2p chain, thus providing the complete primary structure of the lipoyl domain, the E1p/E3-binding domain and the regions of polypeptide chain, probably highly flexible in nature, that link the domains to each other and to the inner-core (E2p-binding) domain. Several of the proteolytically sensitive sites were also identified. The sequence of the B. stearothermophilus E2p chain shows close homology with the sequences of the E2p and E2o chains from E. coli, although significant differences in structure are apparent. Detailed evidence for the sequence of the peptides obtained by limited proteolysis and further chemical and enzymic cleavages have been deposited as Supplementary Publication SUP 50142 (11 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 6BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.

The computerized derivation of rate equations for enzyme reactions on the basis of the pseudo-steady-state assumption and the rapid-equilibrium assumption.

A computer program is developed for the derivation of the rate equation for enzyme reactions on the basis of the pseudo-steady-state assumption and the combination of the pseudo-steady-state and the rapid-equilibrium assumptions. The program not only has an easy input method, but also can obtain a complete rate equation in itself on only one run. The usefulness of the program is demonstrated by deriving the rate equations for some typical enzyme reactions. Details of the program have been deposited as Supplementary Publication SUP 50141 (42 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988), 249, 5.

The cDNA and protein sequences of human lactate dehydrogenase B.

Human lactate dehydrogenase B (LDH-B) cDNA was isolated and sequenced. The LDH-B cDNA insert consists of the protein-coding sequence (999 bp), the 5' (54 bp) and 3' (203 bp) non-coding regions, and the poly(A) tail (50 bp). The predicted sequence of 333 amino acid residues was confirmed by amino acid composition and/or sequence analyses of a total of 185 (56%) residues from tryptic peptides of human LDH-B protein. The nucleotide and amino acid sequences of the human LDH-B coding region show 68% and 75% homologies respectively with those of the human LDH-A. The peptide map and amino acid composition data have been deposited as Supplementary Publication SUP 50139 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

Semisynthetic human [[3H2]Phe1]proinsulin.

Biosynthetic human proinsulin (obtained by recombinant DNA techniques) was used as the starting material for the preparation, by semisynthetic methods, of [3H]proinsulin with the label at the N-terminal phenylalanine residue. The labelled proinsulin was characterized by its retention time on reversed-phase h.p.l.c., by polyacrylamide-gel electrophoresis, by the time course of its enzymic conversion into insulin and by chromatographic analysis after extensive proteolytic degradation. The specific radioactivity of the product was 5 Ci/mmol. Experimental details of the preparation of human [[3H]Phe1]proinsulin, the isolation of this product by isocratic h.p.l.c. and gel filtration, and further characterization of protein intermediates have been deposited as supplement SUP 50138 (12 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on prepayment [see Biochem. J. (1987) 241, 5].

An extremely thermostable extracellular proteinase from a strain of the archaebacterium Desulfurococcus growing at 88 degrees C.

An organism growing at 88 degrees C that closely resembles Desulfurococcus mucosus produced a single extracellular proteinase. We have purified this enzyme and carried out a preliminary characterization. The proteinase, which is a serine-type enzyme, had a molecular mass of 52,000 Da by SDS/polyacrylamide-gel electrophoresis, but only 10,000-13,000 Da by gel-permeation chromatography. Molecular mass values from sucrose-gradient centrifugation were of the same order as those from SDS/polyacrylamide-gel electrophoresis. It had an isoelectric point of 8.7, and was inhibited by di-isopropyl phosphorofluoridate, phenylmethanesulphonyl fluoride and chymostatin. Substrate-specificity studies suggested a possible preference for hydrophobic residues on the C-terminal side of the splitting point. The thermostability of this enzyme is probably greater than any other reported proteinase (t1/2 at 95 degrees C, 70-90 min; t1/2 at 105 degrees C, 8-9 min). Ca2+ chelation does not appear to be implicated in stabilization of the protein structure. The stability of the Desulfurococcus proteinase was not greatly affected by the presence of reducing reagents (e.g. dithiothreitol), some chaotropic agents (e.g. NaSCN) and some detergents, but activity was lost rapidly at 95 degrees C in the presence of the oxidizing agent NaBO3. Proteolytic activity was readily detected at temperatures up to and including 125 degrees C, although denaturation was very rapid above 115 degrees C. A number of Figures supporting some of the findings reported in this paper have been deposited in supplement SUP 50137 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1987) 241, 5.

The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis.

The amino acid sequence of the principal soluble cytochrome c from the phototrophic acidophilic bacterium Rhodopseudomonas (or Rhodopila) globiformis was determined. By the criteria of percentage sequence identity and fewness of internal insertions and deletions it is more similar in sequence to some mitochondrial cytochromes c than to any known bacterial cytochrome. The organism does not have any properties that commend it as being particularly similar to postulated prokaryotic precursors of the mitochondrion. We consider that the relatively high degree of sequence similarity is an instance of convergence, and is an example of the limitations that are imposed on attempts to deduce distant evolutionary relationships from sequence information. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50136 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].

Affinity purification of seminalplasmin and characterization of its interaction with calmodulin.

Bull seminalplasmin antagonizes with high potency and selectivity the activating effect of calmodulin on target enzymes [Gietzen & Galla (1985) Biochem. J. 230, 277-280]. In the present paper we establish that seminalplasmin forms a 1:1, Ca2+-dependent and urea-resistant complex with calmodulin. The dissociation constant equals 1.6 nM. In the absence of Ca2+ a low-affinity complex is formed that is disrupted by 4 M-urea. On the basis of these properties, a fast affinity purification of seminalplasmin was developed. The high specificity of seminalplasmin as a calmodulin antagonist was demonstrated for the multipathway-regulated adenylate cyclase of bovine cerebellum. Far-u.v. c.d. properties are consistent with a random form of seminalplasmin in aqueous solution; 23% alpha-helix is induced on interaction with calmodulin. The fluorescence properties of the single tryptophan residue of seminalplasmin are markedly changed on formation of the complex. These studies allowed us to locate tentatively the peptide segment that interacts with calmodulin, and to ascertain the structural homology between seminalplasmin and other calmodulin-binding peptides. Additional material, showing the inhibition of calmodulin-mediated activation of bovine brain phosphodiesterase by melittin and seminalplasmin and also the near-u.v. spectrum of affinity-purified seminalplasmin, has been deposited as supplement SUP 50135 (4 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1986) 233, 5.

Structure of guanidinium bicarbonate: a model for the bicarbonate anion binding site of the transferrins

Structure of guanidinium bicarbonate: a model for the bicarbonate anion binding site of the transferrins

A neutron diffraction and electron microscopy examination of barium bromide–barium chloride (2/1)

A neutron diffraction and electron microscopy examination of barium bromide–barium chloride (2/1)

Structure of heptaaquacalcium salt of the polymeric hexabromodicadmate(II) anion

[Ca(H20)7][Cd2Br6] , M r = 8 7 0 . 4 4 , monoclinic, P2~/c {Hall symbol P2~c [Acta Cryst. (1981), A37, 517-525]}, a = 8 . 0 7 9 ( 2 ) , b = 1 8 . 6 7 7 ( 6 ) , c = 12.176 (5) A, f l = 96.60 (3) °, v = 1825.08 A 3, z = 4 , D x = 3.17 Mg m -3, Mo K a radiation, 2 = 0.7107 A, /a = 9.95 mm -~, F(000) = 1584, T = 198 K, R = 0.065 for 2259 reflections. The sample was prepared from a saturated solution containing a 1:1.5 molar mixture Ca of CaBr 2 and CdBr 2. When the sealed container was Ca(l) opened to the air the crystals which had originally Cd(2) formed dissolved and colourless crystals of the title Cd(3) Br(l) compound appeared. The structure consists of discrete Br(2) Ca(H20) 2+ ions ( C a O = 2 .36-2 .47 A) hydrogen Br(3) Br(4) bonded to an infinite Cd2Br 2anion extended along the Br(5) a axis. One Cd is octahedraUy coordinated ( C d Br(6) B r = 2 .75-2 .81 A). It shares edges with two crystalo(1) 0(2) lographica l ly equivalent CdBr 6 octahedra and shares o(3) corners with two CdBr 4 tetrahedra ( C d B r = 2 .53 0(4) 2.61 A). 0(5) o(6) 0(7) Experimental. A crystal 0.5 x 0.3 x 0.3 mm sealed in a thin-walled quartz capillary, Nicolet P2~ diffractometer equipped with a Nicolet LT1 cooling device. Unit cell from 15 strong reflections in the range 20 < 0 < 30 °. No absorption correction was used. Intensities for 2665 reflections in the range 8 < h < 8, 0 < k < 20, 0 < l < 13 (20 < 45°). The standard reflections (~,15 and 272) showed non-systematic variations of about 1%. Equivalent reflections were averaged (R = 0.021) to give 2259 unique reflections. Structure by direct methods (MULTAN80, Main et al., 1980), scale factor, weighting factor (k) and all variable (non-hydrogen) positional and anisotropic displacement parameters refined with SHELX76 (Sheldrick, 1976), w = [o'2(F) + kFo2] -1/2 [where k = 0.0035 and tr(F) is the error derived from counting statistics] to give R = 0 . 0 6 5 , wR = 0 0 7 6 and a goodness of fit of S = 1.02. The average sh i f t /e . s .d .=0 .01 ( m a x . = 0.03). Hydrogen atoms could not be located on the final difference map where the largest feature was 2-13 and the smallest --1.67 e A -3. Atomic scattering factors from International Tables for X-ray Crystallography (1974). Atomic coordinates are given in Table 1.* The * Lists of structure factors and anisotropic thermal parameters have been deposited with the British Library Lending Division as Supplementary Publication No. SUP 42812 (13 pp.). Copies may be obtained through The Executive Secretary, International Union of Crystallography, 5 Abbey Square, Chester CH 1 2HU, England. principal interatomic distances are listed in Table 2 and the structure is illustrated in Fig. 1. Table 1. Atomic positions (x l04 ) and equivalent isotropic displacement parameters (A2 x 104)

The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments

Component 8c-1, one of four highly homologous component-8 subunit proteins present in the microfibrils of wool, was isolated as its S-carboxymethyl derivative and its amino acid sequence was determined. Large peptides were isolated after cleaving the protein chemically or enzymically and the sequence of each was determined with an automatic Sequenator. The peptides were ordered by sequence overlaps and, in some instances, by homology with known sequences from other component-8 subunits. The C-terminal residues were identified by three procedures. Full details of the various procedures used have been deposited as Supplementary Publication SUP 50133 (4 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1986) 233, 5. The result showed that the protein comprises 412 residues and has an Mr, including the N-terminal acetyl group, of 48,300. The sequence of residues 98-200 of component 8c-1 was found to correspond to the partial or complete sequences of four homologous type I helical segments previously isolated from helical fragments recovered from chymotryptic digests of microfibrillar proteins of wool [Crewther & Dowling (1971) Appl. Polym. Symp. 18, 1-20; Crewther, Gough, Inglis & McKern (1978) Text. Res. J. 48, 160-162; Gough, Inglis & Crewther (1978) Biochem. J. 173, 385]. Considered in relation to amino acid sequences of other intermediate-filament proteins, the sequence is in accord with the view that keratin filament proteins are of two types [Hanukoglu & Fuchs (1983) Cell (Cambridge, Mass.) 33, 915-924]. Filament proteins from non-keratinous tissues, such as desmin, vimentin, neurofilament proteins and the glial fibrillary acidic protein, which form monocomponent filaments, constitute a third type. It is suggested that as a whole the proteins from intermediate filaments be classed as filamentins, the three types at present identified forming subgroups of this class. The significant homologies between types I, II and III occur almost exclusively in segments of the chain that have been identified as having a coiled-coil structure together with the relatively short sections connecting these segments. The non-coiled-coil segments at the C- and N-termini show no significant homology between types, nor is homology in these segments apparent in all members of one type. Component 8c-1 does not show homology in its terminal segments with the known sequence of any other filamentin.(ABSTRACT TRUNCATED AT 400 WORDS)

The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus.

The amino acid sequence of the cytochrome c-555 from the obligate methanotroph Methylococcus capsulatus strain Bath (N.C.I.B. 11132) was determined. It is a single polypeptide chain of 96 residues, binding a haem group through the cysteine residues at positions 19 and 22, and the only methionine residue is a position 59. The sequence does not closely resemble that of any other cytochrome c that has yet been characterized. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50131 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

Serials at the British Library Lending Division

The British Library Lending Division has one of the largest collections of serials in the world. This paper outlines the history of serials at Boston Spa and describes various aspects of policy and procedures relating to serials, including selection, acquisition, record creation, automation, usage and binding. It concludes by considering the future role of the Lending Division in the light of continuing developments in electronic publishing and telecommunications.

Structure of methyl (4'S,16S)-3β-acetoxy-17-oxospiro[5-androstene-16,3'-(4,5-dihydropyrazole)]-4'-carboxylate

C25H34N2Os, M r--442.54, monoclinic, P2~, a = 6 . 4 1 4 ( 1 ) , b=9 .729 (2 ) , c = 1 9 . 1 9 2 ( 3 ) A , f l= 91.09 (1) °, V = 1197.4 (4) A 3, Z = 2, Dx= 1.227 (1) Mg m -a, Mo Ka, 2 = 0.71069 fi,, g = 0.796 mm -~, F(000)=476, T = 293 K, final R = 0-035 for 1150 independent reflections. The configurations at chiral centers 4' and 16 (3')were found to be both S, assuming the S configuration at 13. The bowing of ring A relative to the remainder of the steroid nucleus is 17.03 (2) ° . The rings have the following conformations: A chair; B half chair; C slightly deformed chair; D slightly distorted envelope. Introduetion. In the course of investigations on steroidal lactones having cytostatic properties (Koc6r, Kabat, Wicha & Peczyfiska-Czoch, 1983), the title compound was synthesized by treatment of (E)-3fl,17fl-dihydroxy-5-androsten16-ylidenacetic acid with diazomethane followed by acetylation of the hydroxy group at C(3). The sequence of atoms in the dihydropyrazole ring thus formed was elucidated from the ~H NMR data. However, the configuration at the new chiral centers 16 (3') and 4' could not be established and therefore X-ray structural analysis of the title compound was necessary. Experimental. Crystal (0.25 x 0.36 x 0.67 mm) from methanol. CAD-4D diffractometer (Enraf-Nonius), MoKu radiation. Cell constants refined from 25 reflections (13.3 2tr I. Equivalent reflections averaged automatically by SDP system, Rln t not estimated. Lorentz and polarization, no absorption correction. Space group P2 r Structure solved by direct methods (MUL TAN80; Main et al., 1980). Mean atomic scattering factors taken from International Tables for X-ray Crystallography (1974). Non-H-atom parameters refined anisotropically for one enantio0108-2701/85/111630-03501.50 morph by a full-matrix procedure (XRAY70 system; Stewart, Kundell & Baldwin, 1970) for 1150 observed F's. H-atom positions found from Ap maps, added and refined (damping 0.3) in the last refinement step (B = Beq of adjacent atom + 1A 2, invariant). Final R = 0.035 (wR = 0.033, unit weights) at A/tr < O. 1. Max. and min. electron densities on final Ap map 0.3 and 0 . 2 e A -3, respectively. Programs used for calculations of secondary results were RING (Phrkfinyi, 1979) and PLALIN (Nardelli, Musatti, Domiano & Andreetti, 1978). Computations done on PDP8/I 1, Cyber-73 and MERA-400 computers. Discussion. Table 1 gives the fractional coordinates of non-hydrogen atoms.* The bond lengths and valence angles are given in Table 2. Fig. 1 presents a projection of the steroid molecule oriented at optimal viewing. In the description of the molecular structure of the steroid under investigation the conventions applied by Duax & Norton (1975) are followed. Fig. 2 shows a view of the steroid parallel to the least-squares plane through the atoms C(1) to C(17) (rings B, C and D). The bowing angle of ring A with respect to this plane (A/B-C-D) is 17.03 (2) °. The mean values of C C bond lengths and C C C angles in saturated rings A and C are 1.536 (8)/k and 111.0 (4) °, respectively. For the unsaturated ring B, the mean value for single C C bond lengths is 1.533 (7)/k with the mean angle of 111.6 (4) °. All bond lengths and angles in rings A, B and C are in agreement (within twice the e.s.d.) with the mean values for 13 AS-steroid structures quoted by Duax & Norton (1975) with two exceptions: bonds C(9)-C(11) and C(13)C(14) (ring C) deviate by more than 0.03 A, being longer and shorter, respectively. * Lists of structure factors, hydrogen-atom positions, anisotropic thermal parameters and torsion angles have been deposited with the British Library Lending Division as Supplementary Publication No. SUP 42348 (15 pp.). Copies may be obtained through The Executive Secretary, International Union of Crystallography, 5 Abbey Square, Chester CH 1 2HU, England. © 1985 International Union of Crystallography GLUZIlqSKI, KRAJEWSKI, URBAlqCZYK-LIPKOWSKA, ARGAY A N D P/~RK/~NYI 1631 Ring A of the steroid reported here may be characterized by a chair conformation ~°C 3 (4C 0. The asymmetry parameters are: AC] = 5.6 (6) ° and AC~z ,2 = 3.0 (6) °. Since the deviations of C(3) and C(10) from the least-squares plane of A [defined by C(1), C(2), C(4) and C(5)] are nearly symmetrical [+0.656 (6)/k], an almost ideal chair conformation with mean torsion angle of 54.6 (6) ° may be assumed. The O-acetyl substituent at C(3) is found in the equatorial position. The unsaturated ring B has the half-chair conformation 8H 9. The asymmetry parameter dCSz,6= 0.8 (7) °. The deviations of C(8) and C(9) from the Table 1. Fractional atomic coordinates (× 10 4) with e.s.d. 's in parentheses Origin along b specified by keeping y of O(1) fixed.

Microcomputer application in a library for document ordering and delivery

The CSTI Document Delivery Service (DDS) of the South African Council for Scientific and Industrial Research (CSIR) was compelled to examine alternative systems for request handling, record keeping and invoicing when its manual system could no longer cope with the ever increasing volume of requests. A fully computerised system on microcomputer was chosen and developed by a senior programmer in the Institute. It is now possible for a relatively small staff to handle the large and increasing volume of requests routinely and with ease. The system is also used for in‐house invoicing, accounts queries, credit control and automatic generation of statistics for record keeping and forward planning. This system has proved to be very flexible and it has led to a number of initially unforeseen advantages. One such advantage is electronic request transmission to the British Library Lending Division (BLLD) on its Automatic Request Transmission (ARTTel) system. Another is the possibility of using a similar system for the transmission of requests to the CSIR's Scientific Liaison Offices overseas. The link to the CSIR computer network also presents the possibility of using the DDS microcomputer as a terminal on the mainframe for archival purposes and for accessing the electronic mail service.