Abstract
The Fab fragment of an antibody, made against an E2-specific feline infectious peritonitis virus neutralizing antibody, has been crystallized in a form suitable for X-ray diffraction analysis from PEG 4000 using vapor diffusion methods. The Fab fragment crystals diffract to about 2·9 Å resolution and are of triclinic space group P1. Unit cell dimensions, by which the reciprocal lattice can be indexed, are a = 57·16 A ̊ , b = 70·85 A ̊ , c = 75·81 A ̊ , α = 85·11∘ , β = 121·28∘ and γ = 116·33∘. There are two Fab fragments comprising the asymmetric unit of the crystals. The presence of a pseudo-mirror plane in the diffraction pattern suggests the presence of at least an approximate dyad axis relating the two Fab fragments within the asymmetric unit.
Highlights
The Fab fragment of an antibody, made against an EZ-specific feline infectious peritonitis virus neutralizing antibody, has been crystallized in a form suitable for X-ray diffraction analysis from PEG 4000 using vapor diffusion methods
These antibodies were conjugated to keyhole limpet hemocyanin (KLH) and hybridomas were generated from conjugate-immunized mice once the anti-Abl response was detected
Antibodies, including those whose crystallizat.ion we report here, were isolated and purified by ion exchange chromatography and characterized with regard to specificity by Western. and competitive Western, blot analyses
Summary
The Fab fragment of an antibody, made against an EZ-specific feline infectious peritonitis virus neutralizing antibody, has been crystallized in a form suitable for X-ray diffraction analysis from PEG 4000 using vapor diffusion methods. Title Characterization of crystals of an Fab fragment of a murine monoclonal antibody. Characterization of Crystals of An Fab Fragment of a Murine Monoclonal Antibody
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