Crystallization and preliminary X-ray diffraction study of the bacterially expressed Fv from the monoclonal anti-lysozyme antibody D1.3 and of its complex with the antigen, lysozyme

Journal of Molecular Biology
G BoulotR J Poljak

Abstract

The associated heavy (VH) and light (VL) chain variable domains (Fv) of the monoclonal anti-lysozyme antibody D1.3, secreted from Escherichia coli, have been crystallized in their antigen-bound and free forms. FvD1.3 gives tetragonal crystals, space group P4(1)2(1)2 (or P4(3)2(1)2), with a = 90.6 A, c = 56.4 A. The FvD1.3-lysozyme complex crystallizes in space group C2, with a = 129.2 A, b = 60.8 A, c = 56.9 A and beta = 119.3 degrees. The crystals contain one molecule of Fv or of the Fv-lysozyme complex in their asymmetric units and diffract X-rays to high resolution, making them suitable for X-ray crystallographic studies.

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Citations

Mar 1, 1994·Journal of Molecular Recognition : JMR·M Malmqvist
Sep 1, 1995·Journal of Molecular Recognition : JMR·B C BradenR J Poljak
Mar 1, 1995·Pharmaceutica acta Helvetiae·B C BradenR J Poljak
Dec 1, 1991·Molecular Immunology·R J Poljak
Oct 1, 1992·Molecular Immunology·J AnthonyS C Ng
Aug 19, 1993·Biochimica Et Biophysica Acta·S TakedaK Nagayama
Jun 6, 2000·Advanced Drug Delivery Reviews·H R Hoogenboom de Haard H
May 5, 2000·Biomolecular Engineering·A Skerra, T G Schmidt
Feb 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·T N BhatR J Poljak
Aug 5, 1997·Proceedings of the National Academy of Sciences of the United States of America·F A GoldbaumR A Mariuzza
Jan 1, 1993·Cancer Investigation·U Kummer, U D Staerz
Apr 2, 2002·Protein Expression and Purification·Reinhard GrisshammerAwinder K Sohal
Jan 19, 2010·MAbs·Thomas SchirrmannStefan Dübel
Jan 24, 1991·Nature·G Winter, C Milstein
Sep 29, 1995·Annals of the New York Academy of Sciences·B C BradenX Ysern

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