Crystallization and preliminary X-ray studies of the VL domain of the antibody McPC603 produced in Escherichia coli

Journal of Molecular Biology
R GlockshuberA Plückthun

Abstract

The VL domain, obtained from a recombinant Fv fragment of the antibody McPC603 expressed in Escherichia coli, has been crystallized as a dimer from 2 M-(NH4)2SO4 (pH 4.0). The crystals are hexagonal, space group P6(1)22. The cell dimensions are a = b = 86.48 A, c = 76.64 A, with a VL monomer as the asymmetric unit. The crystals diffract to 2.0 A. The structure was solved by Patterson search using the VL domain of the Fab fragment of McPC603 and the VL dimer REI.

References

Feb 19, 1975·Biophysics of Structure and Mechanism·H FehlhammerH J Schramm
Feb 13, 1990·Biochemistry·R GlockshuberA Plückthun
Jan 1, 1988·Annual Review of Immunology·P M AlzariR J Poljak
Aug 20, 1986·Journal of Molecular Biology·Y SatowD R Davies
Nov 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·D M SegalD R Davies
Jul 5, 1983·Journal of Molecular Biology·W FureyM Sax

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Citations

Apr 1, 1991·Current Opinion in Biotechnology·A Plückthun
Jun 6, 2000·Advanced Drug Delivery Reviews·H R Hoogenboom de Haard H
Aug 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·X M HeD C Carter
Feb 3, 2005·Current Opinion in Nephrology and Hypertension·Paul W Sanders
Dec 27, 1991·Annals of the New York Academy of Sciences·A Plückthun, I Pfitzinger
Apr 15, 2011·Kidney International·Kolitha BasnayakePaul Cockwell
Oct 4, 1990·Nature·A Plückthun
Sep 22, 2012·Journal of the American Society of Nephrology : JASN·Paul W Sanders

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