Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase

被引:9
作者
Peeraer, Y
Rabijns, A
Verboven, C
Collet, JF
Van Schaftingen, E
De Ranter, C
机构
[1] Katholieke Univ Leuven, Fac Pharmaceut Sci, Lab Analyt Chem & Med Physicochem, B-3000 Louvain, Belgium
[2] Catholic Univ Louvain, Christian de Duve Inst Cellular Pathol, Physiol Chem Lab, B-1200 Brussels, Belgium
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444901017310
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Phosphoserine phosphatase (PSP), a human enzyme involved in the l-serine biosynthesis pathway, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03 Angstrom, b = 130.25 Angstrom, c = 157.29 Angstrom. Calculation of the Matthews coefficient indicates that there are two molecules in the asymmetric unit. A complete native data set to a resolution of 1.53 Angstrom has been collected at 100 K using synchrotron radiation.
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页码:133 / 134
页数:2
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