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

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 213卷 / 04期

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.

引用

页码：617 / 619

页数：3

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