Crystallization and preliminary crystallographic analysis of creatininase from Pseudomonas putida

被引：3

作者：

Beuth, B ^{[1
]}

Niefind, K ^{[1
]}

Schomburg, D ^{[1
]}

机构：

[1] Univ Cologne, Inst Biochem, D-50674 Cologne, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷

关键词：

D O I：

10.1107/S0907444902009447

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Creatininase (CrnA) from Pseudomonas putida is a homohexameric heat-stable enzyme composed of 259 amino acids per subunit. The molecular weight of each monomer is 28.4 kDa. The enzyme hydrolyses creatinine to yield creatine. Crystals of this protein have been grown from ethanol/PEG 8000. They belong to the monoclinic space group P2(1), with unit-cell parameters a = 74.8, b = 95.7, c = 116.9 Angstrom, beta = gamma = 90, beta = 103.8degrees. The diffraction limit is 2.5 Angstrom. The self-rotation function of the native data set is consistent with a CrnA hexamer in the asymmetric unit and suggests D-3 point-group symmetry of the enzyme.

引用

页码：1356 / 1358

页数：3

共 13 条

[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].