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Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus
1Research School of Chemistry, Australian National University, GPO Box 414, Canberra, ACT 2601, Australia.
Abstract:
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 alpha/beta hydrolase fold. The crystals diffract to 2.8 A and belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 A.
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