CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDY OF THE BACTERIALLY EXPRESSED FV FROM THE MONOCLONAL ANTILYSOZYME ANTIBODY D1.3 AND OF ITS COMPLEX WITH THE ANTIGEN, LYSOZYME

被引:58
作者
BOULOT, G [1 ]
EISELE, JL [1 ]
BENTLEY, GA [1 ]
BHAT, TN [1 ]
WARD, ES [1 ]
WINTER, G [1 ]
POLJAK, RJ [1 ]
机构
[1] MRC,MOLEC BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND
关键词
D O I
10.1016/S0022-2836(05)80248-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 P41212 (or P43212), with a = 90·6 Å, c = 56·4 Å. The FvD1.3-lysozyme complex crystallizes in space group C2, with a = 129·2 Å, b = 60·8 Å, c = 56·9 Å and β = 119·3°. 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. © 1990 Academic Press Limited.
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页码:617 / 619
页数:3
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