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Crystallization and preliminary crystallographic analysis of recombinant human P38 MAP kinase.
Authors:S. Pav   D. M. White   S. Rogers   K. M. Crane   C. L. Cywin   W. Davidson   J. Hopkins   M. L. Brown   C. A. Pargellis     L. Tong
Affiliation:Department of Inflammatory Diseases, Boehringer Ingelheim Pharmaceuticals, Inc. Ridgefield, Connecticut 06877, USA.
Abstract: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.
Keywords:crystallization  mitogen-activated protein kinase (MAPK)  p38  RK  serine/threonine kinase  X-ray diffraction
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