Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1

被引:1
|
作者
Bong, Seoung Min [1 ]
Yang, Seung Won [1 ]
Choi, Ji-Woong [1 ]
Kim, Seung Jun [2 ]
Lee, Byung Il [1 ]
机构
[1] Natl Canc Ctr, Res Inst, Div Convergence Technol, Biomol Funct Res Branch, Goyang 411769, Gyeonggi, South Korea
[2] Korea Res Inst Biosci & Biotechnol, Med Prote Res Ctr, Taejon 305806, South Korea
基金
新加坡国家研究基金会;
关键词
myotubularin; MTMR; phosphatidylinositol; phosphatase; FAMILY; PHOSPHATASES; MTMR2;
D O I
10.1107/S2053230X15000606
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Myotubularin-related protein 1 is a phosphatase that dephosphorylates phospholipids such as phosphatidylinositol 3-phosphate or phosphatidylinositol 3,5-bisphosphate. In this study, human MTMR1 was overexpressed in Escherichia coli, purified and crystallized at 277 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 2.0 angstrom resolution using synchrotron radiation. The crystals belonged to space group P1, with unit-cell parameters a = 67.219, b = 96.587, c = 97.581 angstrom, alpha = 87.597, beta = 86.072, gamma = 77.327 degrees. Assuming the presence of four molecules in the asymmetric unit, the calculated Matthews coefficient value was 2.61 angstrom 3 Da(-1) and the corresponding solvent content was 52.9%.
引用
收藏
页码:261 / 265
页数:5
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