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Crystallization and preliminary crystallographic analysis of recombinant human p38 MAP kinase
Author(s) -
Pav S.,
White D.M.,
Rogers S.,
Crane K.M.,
Cywin C.L.,
Hopkins J.,
Brown M.L.,
Pargellis C.A.,
Tong L.,
Davidson W.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060126
Subject(s) - recombinant dna , crystallization , crystal (programming language) , sf9 , crystallography , resolution (logic) , escherichia coli , chemistry , biochemistry , gene , organic chemistry , artificial intelligence , spodoptera , computer science , programming language
The recombinant human p38 MAP kinase has been expressed and purified from both Escherichia coli and SF9 cells, and has been crystallized in two forms by the hanging drop vapor diffusion method using PEG as precipitant. Both crystal forms belong to space group P 2 1 2 1 2 1 . The cell parameters for crystal form 1 are a = 65.2 Å, b = 74.6 Å and c = 78.1 Å. Those for crystal form 2 are a = 58.3 Å, b = 68.3 Å and c = 87.9 Å. Diffraction data to 2.0 Å resolution have been collected on both forms.