Crystallization and initial X-ray analysis of rabbit mature sterol carrier protein 2

被引:6
作者
Choinowski, T [1 ]
Dyer, JH [1 ]
Maderegger, B [1 ]
Winterhalter, KH [1 ]
Hauser, H [1 ]
Piontek, K [1 ]
机构
[1] Swiss Fed Inst Technol, Inst Biochem, CH-8092 Zurich, Switzerland
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷
关键词
D O I
10.1107/S0907444999007106
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Sterol carrier protein 2 (SCP2) is a basic intracellular protein which facilitates the in vitro intermembrane transfer of cholesterol, phospholipids and glycolipids. SCP2 was expressed in Escherichia coli, purified to apparent electrophoretic homogeneity and crystallized. Single crystals were obtained by hanging-drop vapour diffusion using ammonium sulfate as precipitant. These crystals belong to space group P4(1)2(1)2 or its enantiomorph, with unit-cell parameters a = b = 57.5, c = 86.5 Angstrom, and have one molecule in the crystallographic asymmetric unit. Intensity data to 1.8 Angstrom resolution were collected from native SCP2 crystals using synchrotron radiation, were processed and scaled with an R-linear = 4.9%.
引用
收藏
页码:1478 / 1480
页数:3
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