CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF THE VL DOMAIN OF THE ANTIBODY MCPC603 PRODUCED IN ESCHERICHIA-COLI

被引:25
作者
GLOCKSHUBER, R
STEIPE, B
HUBER, R
PLUCKTHUN, A
机构
[1] UNIV MUNICH, GENZENTRUM, W-8033 MARTINSRIED, GERMANY
[2] MAX PLANCK INST BIOCHEM, STRUKTURFORSCH ABT, W-8033 MARTINSRIED, GERMANY
关键词
D O I
10.1016/S0022-2836(05)80247-5
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 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 P6122. The cell dimensions are a=b=86·48 Å, c=76·64 Å, with a VL monomer as the asymmetric unit. The crystals diffract to 2·0 Å. The structure was solved by Patterson search using the VL domain of the Fab fragment of McPC603 and the VL dimer REI. © 1990 Academic Press Limited.
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收藏
页码:613 / 615
页数:3
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