Crystallization and preliminary crystallographic analysis of recombinant human P38 MAP kinase.
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 P2(1)2(1)2(1). The cell parameters for crystal form 1 are a = 65.2 A, b = 74.6 A and c = 78.1 A. Those for crystal form 2 are a = 58.3 A, b = 68.3 A and c = 87.9 A. Diffraction data to 2.0 A resolution have been collected on both forms.
Pav
S
S
Department of Inflammatory Diseases, Boehringer Ingelheim Pharmaceuticals, Inc. Ridgefield, Connecticut 06877, USA. pav@mhv.net
White
D M
DM
Rogers
S
S
Crane
K M
KM
Cywin
C L
CL
Davidson
W
W
Hopkins
J
J
Brown
M L
ML
Pargellis
C A
CA
Tong
L
L
D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000737:chemistry*; D002460:Cell Line; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D020928:Mitogen-Activated Protein Kinases; D011994:Recombinant Proteins / Q000737:chemistry; D018411:Spodoptera; D048051:p38 Mitogen-Activated Protein Kinases
D011994:Recombinant Proteins; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D020928:Mitogen-Activated Protein Kinases; D048051:p38 Mitogen-Activated Protein Kinases