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Preliminary X-ray crystallographic studies of UDP-glucose-4-epimerase from Aspergillus nidulans.

ABSTRACT: UDP-glucose-4-epimerase (GALE) from Aspergillus nidulans was overexpressed in Escherichia coli, purified via His-tag affinity chromatography and cocrystallized with UDP-galactose using the microbatch method. The crystals diffracted to 2.4?Å resolution using synchrotron radiation on the Canadian Light Source 08ID-1 beamline. Examination of the data with d*TREK revealed nonmerohedral twinning, from which a single lattice was ultimately extracted for processing. The final space group was found to be C2, with unit-cell parameters a = 66.13, b = 119.15, c = 161.42?Å, ? = 98.48°. An initial structure solution has been obtained via molecular replacement employing human GALE (PDB entry 1hzj) as a template model.

SUBMITTER: Dalrymple SA

PROVIDER: S-EPMC3151119 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Preliminary X-ray crystallographic studies of UDP-glucose-4-epimerase from Aspergillus nidulans.

Dalrymple Sean A SA Sheoran Inder I Kaminskyj Susan G W SG Sanders David A R DA

Acta crystallographica. Section F, Structural biology and crystallization communications 20110719 Pt 8

UDP-glucose-4-epimerase (GALE) from Aspergillus nidulans was overexpressed in Escherichia coli, purified via His-tag affinity chromatography and cocrystallized with UDP-galactose using the microbatch method. The crystals diffracted to 2.4 Å resolution using synchrotron radiation on the Canadian Light Source 08ID-1 beamline. Examination of the data with d*TREK revealed nonmerohedral twinning, from which a single lattice was ultimately extracted for processing. The final space group was found to b ...[more]

PMID: 21821886

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