CRYSTALLIZATION AND PRELIMINARY STRUCTURAL STUDIES OF A CHORISMATE MUTASE CATALYTIC ANTIBODY COMPLEXED WITH A TRANSITION-STATE ANALOG

被引：6

作者：

HAYNES, MR

STURA, EA

HILVERT, D

WILSON, IA

机构：

[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA

[2] Scripps Res Inst, DEPT CHEM, LA JOLLA, CA 92037 USA

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1994年 / 18卷 / 02期

关键词：

CATALYTIC ANTIBODY; CHORISMATE MUTASE; CRYSTALLIZATION; X-RAY DIFFRACTION;

D O I：

10.1002/prot.340180211

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 Fab' fragment of a catalytic antibody with chorismate mutase activity has been crystallized as a complex with the transition-state analog hapten. The complex was crystallized by the vapor diffusion method using ammonium sulfate as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 37.1 Angstrom, b = 63.3 Angstrom, c = 178.5 Angstrom, and there is one Fab' molecule per asymmetric unit. The crystals diffract X-rays to at least 3.0 Angstrom and are suitable for X-ray crystallographic studies. (C) 1994 Wiley-Liss, Inc.

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页码：198 / 200

页数：3

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