Atomic structure at 2.5 Å resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice

E.Yu Morgunova,A.M Mikhailov,A.N Popov,E.V Blagova,E.A Smirnova,B.K Vainshtein,Ch Mao,Sh.R Armstrong,S.E Ealick,A.A Komissarov,E.V Linkova,A.A Burlakova,A.S Mironov,V.G Debabov

doi:10.1016/0014-5793(95)00489-v

Atomic structure at 2.5 Å resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice

E.Yu Morgunova, A.M Mikhailov + Show 12 more

Open Access

https://doi.org/10.1016/0014-5793(95)00489-v

Copy DOI

Journal: FEBS Letters	Publication Date: Jun 26, 1995
Citations: 52

Affiliation: Russian Academy of Sciences, A.V. Shubnikov Institute of Crystallography, Cornell University

#Monoclinic Crystal Form #Molecular Replacement Method + Show 8 more

Abstract
Full-Text PDF
Similar Papers

Abstract

Uridine phosphorylase from E. coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form. The structure was determined by the molecular replacement method at 2.5 Å resolution. The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%. The amino acid fold of the protein was found to be the same as that in the trigonal crystals. The positions of flexible regions were refined. The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.

Full Text