Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase.
Human acylphosphatase, an 11 kDa enzyme that catalyzes the hydrolysis of carboxyl phosphate bonds, has been studied extensively as a model system for amyloid-fibril formation. However, the structure is still not known of any isoform of human acylphosphatase. Here, the crystallization and preliminary X-ray diffraction data analysis of human common-type acylphosphatase are reported. Crystals of human common-type acylphosphatase have been grown by the sitting-drop vapour-diffusion method at 289 K using polyethylene glycol 4000 as precipitant. Diffraction data were collected to 1.45 A resolution at 100 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.58, b = 47.23, c = 57.26 A.
Yeung
Rachel C Y
RC
Department of Biochemistry, Centre for Protein Science and Crystallography, The Chinese University of Hong Kong, Hong Kong, People's Republic of China.
Lam
Sonia Y
SY
Wong
Kam-Bo
KB
D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D006868:Hydrolysis; D007527:Isoenzymes / Q000737:chemistry; D008099:Liver / Q000201:enzymology; D008956:Models, Chemical; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D007527:Isoenzymes; D011994:Recombinant Proteins; D000097024:Acylphosphatase