Crystallization and preliminary X-ray analysis of the coiled-coil domain of dystrophia myotonica kinase.

Pilar Garcia, Marco Marino, Olga Mayans

Journal: Acta crystallographica. Section D, Biological crystallography 2005;60(Pt 12 Pt 2):2336-9

PMID: 15583383

Full Text on International Union of Crystallography View on PubMed

Abstract

The coiled-coil domain of dystrophia myotonica protein kinase (DMPK) has been cloned, overexpressed, purified and crystallized. Two crystal forms have been obtained that belong to space groups P3 and P2(1)2(1)2(1) and diffract to 2.4 and 1.6 A resolution, respectively. Experimental phases were obtained by MAD from an SeMet derivative. The location of selenium sites used molecular-replacement phases obtained from search models lacking sequence similarity with the coiled-coil under study. Both crystal forms contain three polypeptide chains in the asymmetric unit.

Address: Division of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

DOI: 10.1107/S0907444904026873

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MeSH Terms: Crystallization, Crystallography, X-Ray, Escherichia coli, Humans, Models, Chemical, Models, Molecular, Myotonin-Protein Kinase, Peptides, Plasmids, Protein Conformation, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Recombinant Proteins, Selenium, Temperature