Purification, crystallization and preliminary crystallographic analysis of Est25: a ketoprofen-specific hormone-sensitive lipase

被引：7

作者：

Kim, SeungBum

Joo, Sangbum

Yoon, Hyun C.

Ryu, Yeonwoo

Kim, Kyeong Kyu

Kim, T. Doohun ^{[1
]}

机构：

[1] Ajou Univ, Coll Engn, Dept Biol & Mol Engn, Suwon 441749, South Korea

[2] Sungkyunkwan Univ, Sch Med, Dept Mol Cell Biol, Suwon, South Korea

来源：

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

关键词：

D O I：

10.1107/S1744309107026152

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Ketoprofen, a nonsteroidal anti-inflammatory drug, inhibits the synthesis of prostaglandin. A novel hydrolase (Est25) with high ketoprofen specificity has previously been identified using a metagenomic library from environmental samples. Recombinant Est25 protein with a histidine tag at the N-terminus was expressed in Escherichia coli and purified in a homogenous form. Est25 was crystallized from 2.4 M sodium malonate pH 7.0 and X-ray diffraction data were collected to 1.49 angstrom using synchrotron radiation. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 197.8, b = 95.2, c = 99.4 angstrom, beta = 97.1 degrees.

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页码：579 / 581

页数：3

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