Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1

被引：3

作者：

An, Young Jun ^{[1
,2
]}

Lee, Chang-Ro ^{[1
]}

Supangat, Supangat ^{[1
]}

Lee, Hyun Sook ^{[1
]}

Lee, Jung-Hyun ^{[1
,3
]}

Kang, Sung Gyun ^{[1
,3
]}

Cha, Sun-Shin ^{[1
,3
]}

机构：

[1] Korea Ocean Res & Dev Inst, Marine Biotechnol Res Ctr, Ansan 426744, South Korea

[2] Myongji Univ, Dept Biol Sci, Yongin 449728, South Korea

[3] Univ Sci & Technol, Dept Marine Biotechnol, Taejon 305333, South Korea

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷

关键词：

ATP-DEPENDENT PROTEASE; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; PROTEOLYTIC DOMAIN; QUALITY-CONTROL; ACTIVE-SITE; RESOLUTION; BACTERIAL; PROTEINS; REVEALS;

D O I：

10.1107/S1744309109048039

中图分类号：

Q5 [生物化学];

学科分类号：

070307 [化学生物学];

摘要：

Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from Thermococcus onnurineus NA1 was purified and crystallized at 295 K. A 2.0 angstrom resolution data set was collected using synchrotron radiation. The crystals belonged to space group P6(3), with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 angstrom. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

引用

页码：54 / 56

页数：3

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