1. Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii
- Author
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Kam-Bo Wong, Mark D. Allen, Yuk-Yin Cheung, and Mark Bycroft
- Subjects
biology ,Sodium formate ,Molecular Sequence Data ,General Medicine ,Phosphate ,biology.organism_classification ,Acylphosphatase ,Crystallography, X-Ray ,law.invention ,Acid Anhydride Hydrolases ,chemistry.chemical_compound ,Hydrolysis ,Amyloid disease ,Crystallography ,Pyrococcus horikoshii ,chemistry ,Structural Biology ,law ,Carbamoyl phosphate ,Animals ,Amino Acid Sequence ,Crystallization ,Sequence Alignment - Abstract
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 P3(2)21, with unit-cell parameters a = b = 85.65, c = 75.51 A. The asymmetric unit contains two molecules of acylphosphatase, with a corresponding crystal volume per protein weight of 3.9 A Da(-1) and a solvent content of 68.6%. A data set diffracting to 1.6 A resolution was collected from a single crystal at 100 K.
- Published
- 2004