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Protein Science, Vol 6, Issue 1 242-245, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary crystallographic analysis of recombinant human p38 MAP kinase

S. PAV, D. M. WHITE, S. ROGERS, K. M. CRANE, C. L. CYWIN, W. DAVIDSON, J. HOPKINS, M. L. BROWN, C. A. PARGELLIS and L. TONG
Department of Inflammatory Diseases, Boehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, P.O. Box 368, Ridgefield, Connecticut 06877

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.
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