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

Jian-Wei Liu; Denis Verger; Paul D. CarrHong YangDavid L. Ollis

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

机译：表达、纯化和初步的hyperthermophilic晶体研究

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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 A and belong to space group I222 ro I2_12_12_1, with unit-cell parameters α = 155.6, b = 155.0, c = 162.4 A.

机译：的酯酶hyperthermophilic archeonArchaeoglobus fulgidus已经表示,适用于纯化和结晶形式结构分析。35 467 Da和显示序列相似性的质量其他酯酶具有α/β水解酶。和属于空间群I222 ro I2_12_12_1,晶胞参数α= 155.6,= 155.0 b, c= 162.4。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第7期|900-901|共2页
作者
Jian-Wei Liu; Denis Verger; Paul D. CarrHong YangDavid L. Ollis;
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作者单位

Research School of Chemistry, Australian National University, GPO Box 414, Canberra, ACT 2601, Australia;

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原文格式 PDF
正文语种英语
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Esterases; structured analysis; Molecular weightsPurificationArchaeoglobus fulgidusCrystallization;

机译：酯酶、结构分析、分子weightsPurificationArchaeoglobus;

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

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