Crystallization and preliminary X-ray studies of the protease domain of the heat-shock protein HtrA from Thermotoga maritima

被引：8

作者：

Kim, DY ^{[1
]}

Kim, KK ^{[1
]}

机构：

[1] Sungkyunkwan Univ, Sch Med, SBRI, Ctr Mol Med,Dept Mol Cell Biol, Suwon 440746, South Korea

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2002年 / 58卷

关键词：

D O I：

10.1107/S0907444901018248

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

HtrA (high-temperature requirement A) is a widely distributed heat-shock protein which has both molecular-chaperone and proteolytic activities. It is composed of two PDZ domains essential for oligomerization and a protease domain. To understand the molecular basis of the dual function of HtrA, the protease domain of T. maritima HtrA has been crystallized. X-ray diffraction data have been collected to 2.7 Angstrom resolution using a synchrotron-radiation source. Crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 120.55 (8) Angstrom. The asymmetric unit contains two protease domains, with a corresponding V-M of 2.80 Angstrom (3) Da(-1) and a solvent content of 56.1%.

引用

页码：170 / 172

页数：3

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