Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus
Date
2000
Authors
Liu, Jian-Wei
Verger, Dennis
Carr, Paul D
Yang, Hong
Ollis, David
Journal Title
Journal ISSN
Volume Title
Publisher
Munksgaard International Publishers
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.
Description
Keywords
Keywords: esterase; primer DNA; recombinant protein; Archaeoglobus fulgidus; article; chemistry; enzymology; genetics; ion exchange chromatography; isolation and purification; nucleotide sequence; polyacrylamide gel electrophoresis; protein conformation; X ray crys
Citation
Collections
Source
Acta Crystallographica Section D: Biological Crystallography
Type
Journal article