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 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.
Cheung
Yuk-Yin
YY
Department of Biochemistry, The Chinese University of Hong Kong, Hong Kong.
Allen
Mark D
MD
Bycroft
Mark
M
Wong
Kam-Bo
KB
D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D016415:Sequence Alignment; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000097024:Acylphosphatase