Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii

Acylphosphatases catalyse the hydrolysis of the carboxyl phosphate bond in metabolites such as acetyl phosphate, 1,3‐bisphosphoglycerate, succinoyl phosphate and carbamoyl phosphate. In this study, acylphosphatase (91 residues) from the hyperthermophilic archaeon Pyrococcus horikoshii has been clone...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-07, Vol.60 (7), p.1308-1310
Main Authors: Cheung, Yuk-Yin, Allen, Mark D., Bycroft, Mark, Wong, Kam-Bo
Format: Article
Language:English
Subjects:
Acid Anhydride Hydrolases - chemistry
Acylphosphatase
Amino Acid Sequence
amyloid diseases
Animals
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Pyrococcus horikoshii - enzymology
Sequence Alignment
thermal stability
thermophiles
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Acylphosphatases catalyse the hydrolysis of the carboxyl phosphate bond in metabolites such as acetyl phosphate, 1,3‐bisphosphoglycerate, succinoyl phosphate and carbamoyl phosphate. In this study, acylphosphatase (91 residues) from the hyperthermophilic archaeon Pyrococcus horikoshii has been cloned, overexpressed, purified and crystallized using the sitting‐drop vapour‐diffusion method using sodium formate as a precipitant at 289 K. The crystals belong to space group P3221, with unit‐cell parameters a = b = 85.65, c = 75.51 Å. The asymmetric unit contains two molecules of acylphosphatase, with a corresponding crystal volume per protein weight of 3.9 Å Da−1 and a solvent content of 68.6%. A data set diffracting to 1.6 Å resolution was collected from a single crystal at 100 K.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444904010996