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Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

Liu, Jian-Wei; Verger, Dennis; Carr, Paul D; Yang, Hong; Ollis, David


An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the α/β hydrolase fold. The crystals diffract to 2.8 Å and belong to space group I222 or 1212121, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 Å.

CollectionsANU Research Publications
Date published: 2000
Type: Journal article
Source: Acta Crystallographica Section D: Biological Crystallography
DOI: 10.1107/S0907444900005084


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