Volume 65, Issue 8 pp. 843-845

Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans

Sarathy Karunan Partha

Sarathy Karunan Partha

Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada

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Sara A. Bonderoff

Sara A. Bonderoff

Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada

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Karin E. Van Straaten

Karin E. Van Straaten

Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada

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David A. R. Sanders

David A. R. Sanders

Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada

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First published: 18 August 2009
David A. R. Sanders, e-mail: [email protected]

Abstract

UDP-galactopyranose mutase (UGM) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. A UGM–substrate complex from Deinococccus radiodurans has been expressed, purified and crystallized. Crystals were obtained by the microbatch-under-oil method at room temperature. The crystals diffracted to 2.36 Å resolution at the Canadian Light Source The space group was found to be P212121, with unit-cell parameters a = 134.0, b = 176.6, c = 221.6 Å. The initial structure solution was determined by molecular replacement using UGM from Mycobacterium tuberculosis (PDB code 1v0j) as a template model.

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