Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1

被引：3

作者：

Wang, H

Pang, H

Ding, Y

Li, Y

Wu, X

Rao, ZH ^{[1
]}

机构：

[1] Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China

[2] Chinese Acad Sci, Natl Lab Macromol, Inst Biophys, Beijing 100101, Peoples R China

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷

关键词：

D O I：

10.1107/S174430910501184X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine-salvage pathway and catalyzes the continuous reaction of 2,3-diketo-5-methylthio-1-phosphopentane to yield the acireductone metabolite. Recombinant human E1 enzyme has been crystallized using the hangingdrop vapour-diffusion method and diffraction-quality crystals were grown at 291 K using PEG 4000 as precipitant. Diffraction data were collected to 1.7 angstrom resolution from SeMet-derivative crystals at 100 K using synchrotron radiation. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.02, b = 57.55, c = 87.32 angstrom. The structure was subsequently solved by the multiwavelength anomalous diffraction (MAD) phasing method.

引用

页码：521 / 523

页数：3

共 23 条

[1] Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis [J].