CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF HUMAN CKSHS1 - A CELL-CYCLE REGULATORY PROTEIN

被引：7

作者：

ARVAI, AS

BOURNE, Y

WILLIAMS, D

REED, SI

TAINER, JA

机构：

[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA

[2] FAC MED SECTEUR NORD MARSEILLE, CRISTALLOG & CRISTALLISAT MACROMOLEC BIOL LAB, F-13916 MARSEILLE 20, FRANCE

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1995年 / 21卷 / 01期

关键词：

CELL CYCLE PROTEIN; CRYSTALLIZATION; X-RAY DIFFRACTION;

D O I：

10.1002/prot.340210109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cell cycle regulatory protein CksHs1 has been crystallized in a form suitable for X-ray studies. CksHs1 crystals were grown in the presence of vanadate, a phosphatase inhibitor, but were also obtained with phosphate or tungstate as a cofactor. They belong to the hexagonal space group P6(1)22 with unit cell dimensions: a = b = 94 Angstrom, c = 131,6 Angstrom, and gamma = 120 degrees. The crystals grown in the presence of vanadate diffract X-rays to at least 2.8 Angstrom. Molecular replacement results from the homologous human CksHs2 structure reveal that a dimer forms the crystal habit, giving the unusual V-m value of 4.4 Angstrom(3)/Da or a solvent content of 72%. (C) 1995 Wiley-Liss, Inc.

引用

页码：70 / 73

页数：4

共 11 条

[1]

ARVAI AS, UNPUB

[2] CRYSTAL-STRUCTURE OF HUMAN PROTEIN-TYROSINE-PHOSPHATASE 1B [J].