PURIFICATION AND CRYSTALLIZATION OF THE CATALYTIC DOMAIN OF HUMAN PROTEIN-TYROSINE-PHOSPHATASE 1B EXPRESSED IN ESCHERICHIA-COLI

被引:45
作者
BARFORD, D
KELLER, JC
FLINT, AJ
TONKS, NK
机构
[1] COLD SPRING HARBOR LAB,COLD SPRING HARBOR,NY 11724
[2] WM KECK STRUCT BIOL LAB,COLD SPRING HARBOR,NY 11724
关键词
PROTEIN TYROSINE PHOSPHATASES; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; PROTEIN CRYSTALLOGRAPHY;
D O I
10.1006/jmbi.1994.1409
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 amino-terminal 321 residues encoding the catalytic domain of human protein tyrosine phosphatase 1B (molecular mass 37 kDa) has been expressed in Escherichia coli, purified to homogeneity and crystallized. The crystals diffract to 2.4 Å resolution when exposed to synchrotron radiation and belong to space group P3121 (or its enantiomorph P3221) with α = 88.4 Å, b = 88.4 Å, c = 104.0 Å, α = β = 90.0°, γ = 120.0°. There is one molecule of protein tyrosine phosphatase 1B per asymmetric unit and the crystal form is suitable for the determination of the atomic structure of the enzyme. © 1994 Academic Press Limited.
引用
收藏
页码:726 / 730
页数:5
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