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Crystallization and preliminary crystallographic analysis of human common‐type acylphosphatase

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 Å resolution at 100 K. The crystals belong to space group P212121, with unit‐cell parameters a = 42.58, b = 47.23, c = 57.26 Å. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary crystallographic analysis of human common‐type acylphosphatase

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References (20)

Publisher
Wiley
Copyright
Copyright © 2006 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430910504145X
pmid
16511269
Publisher site
See Article on Publisher Site

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 Å resolution at 100 K. The crystals belong to space group P212121, with unit‐cell parameters a = 42.58, b = 47.23, c = 57.26 Å.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2006

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