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

Jian Wei Liu; Denis Verger; Paul D. Carr; Hong Yang; David L. Ollis

doi:10.1107/S0907444900005084

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

Jian Wei Liu, Denis Verger, Paul D. Carr, Hong Yang, David L. Ollis^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

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 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.

Original language	English
Pages (from-to)	900-901
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	56
Issue number	7
DOIs	https://doi.org/10.1107/S0907444900005084
Publication status	Published - 2000

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

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 α/β hydrolase fold. The crystals diffract to 2.8 {\AA} and belong to space group I222 or 1212121, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 {\AA}.",

author = "Liu, \{Jian Wei\} and Denis Verger and Carr, \{Paul D.\} and Hong Yang and Ollis, \{David L.\}",

year = "2000",

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language = "English",

volume = "56",

pages = "900--901",

journal = "Acta Crystallographica Section D: Biological Crystallography",

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T1 - Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

AU - Liu, Jian Wei

AU - Verger, Denis

AU - Carr, Paul D.

AU - Yang, Hong

AU - Ollis, David L.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0033949669

U2 - 10.1107/S0907444900005084

DO - 10.1107/S0907444900005084

M3 - Article

SN - 0907-4449

VL - 56

SP - 900

EP - 901

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 7

ER -

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

Abstract

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