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Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase.

ABSTRACT: 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.

SUBMITTER: Yeung RC

PROVIDER: S-EPMC2150918 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase.

Yeung Rachel C Y RC Lam Sonia Y SY Wong Kam-Bo KB

Acta crystallographica. Section F, Structural biology and crystallization communications 20051223 Pt 1

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 u ...[more]

PMID: 16511269

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