Crystallization and preliminary X-ray analysis of a hydantoinase from Arthrobacter aurescens DSM 3745

被引：8

作者：

May, O ^{[1
]}

Siemann, M ^{[1
]}

Syldatk, C ^{[1
]}

Niefind, K ^{[1
]}

Schomburg, D ^{[1
]}

机构：

[1] GBF,D-38124 BRAUNSCHWEIG,GERMANY

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1996年 / 52卷

关键词：

D O I：

10.1107/S0907444996007731

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

L-Hydantoinase from Arthrobacter aurescens DSM 3745 has been purified to homogeneity and crystallized from polyethylene glycol solutions in a form suitable for X-ray diffraction analysis. The crystals have been grown by the sitting-drop variant of the vapour-diffusion method. X-ray diffraction studies show that the crystals belong to the monoclinic space group P2(1) with a = 111.2, b = 74.4, c = 146.5 Angstrom and beta = 106.7 degrees. Its asymmetric unit contains four monomers related by 222 symmetry. The crystals diffract to at least 2.6 Angstrom.

引用

页码：1209 / 1210

页数：2

共 17 条

[1]

[Anonymous], ACTA CRYSTALLOGR D

[2]

[Anonymous], BIOCATALYTIC PRODUCT

[3]

Brunger A. T., 1992, X PLOR VERSION 3 1 S

[4]

DUCRUIX A, 1992, CRYSTALLIZATION NUCL, pCH4