Expression, purification, crystallization and preliminary X-ray analysis of the human NORE1 SARAH domain

被引：1
|
作者：
Kim, Hye Jin [1 ,2 ]
Hwang, Eunha [1 ,3 ]
Han, Young-Hyun [1 ]
Choi, Saehae [1 ]
Lee, Woo Cheol [1 ]
Kim, Hye-Yeon [1 ]
Jeon, Young Ho [4 ]
Cheong, Chaejoon [1 ,2 ]
Cheong, Hae-Kap [1 ]
机构：
[1] Korea Basic Sci Inst, Div Magnet Resonance, Ochang 363883, Chungbuk, South Korea
[2] Korea Univ Sci & Technol, Dept Bioanalyt Sci, Taejon 305350, South Korea
[3] Korea Univ, Div Biotechnol, Coll Life Sci & Biotechnol, Seoul 136701, South Korea
[4] Korea Univ, Coll Pharm, Jochiwon 339700, Chungnam, South Korea
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
关键词：
TUMOR-SUPPRESSOR; IDENTIFICATION; PROTEINS; BINDING; PATHWAY;
D O I：
10.1107/S1744309112021744
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
NORE1 is an important tumour suppressor in human cancers that interacts with the pro-apoptotic protein kinase MST1/2 through SARAH domains. The SARAH domain (residues 366-413) of human NORE1 was expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystal diffracted to 2.7 angstrom resolution and belonged to space group P6(1)22, with unit-cell parameters a = b = 73.041, c = 66.092 angstrom, alpha = beta = 90, gamma = 120 degrees.
引用
收藏
页码：813 / 815
页数：3
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