Crystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of Pseudomonas aeruginosa amidase

被引：4

作者：

Andrade, Jorge

Karmali, Amin

Carrondo, Maria A.

Frazao, Carlos

机构：

[1] Univ Tecn Lisboa, Inst Tecnol Quim & Biol, P-2781901 Oeiras, Portugal

[2] Inst Super Engn Lisboa, Ctr Invest Engn Quim & Biotecnol, P-1949014 Lisbon, Portugal

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷

关键词：

D O I：

10.1107/S1744309107005830

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The aliphatic amidase ( acylamide amidohydrolase; EC 3.5.1.4) from Pseudomonas aeruginosa is a hexameric enzyme composed of six identical subunits with a molecular weight of similar to 38 kDa. Since microbial amidases are very important enzymes in industrial biocatalysis, the structural characterization of this enzyme will help in the design of novel catalytic activities of commercial interest. The present study reports the successful crystallization of the wild-type amidase from P. aeruginosa. Native crystals were obtained and a complete data set was collected at 1.4 angstrom resolution, although the crystals showed diffraction to 1.25 angstrom resolution. The crystals were found to belong to space group P6(3)22, with unitcell parameters a = b = 102.60, c = 151.71 angstrom, and contain one molecule in the asymmetric unit.

引用

页码：214 / 216

页数：3

共 27 条

[1] The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing [J].