Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/34362
Title: Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain
Authors: Li, MH
Kwok, F
An, XM
Chang, WR
Lau, CK
Zhang, JP
Liu, SQ
Leung, YC 
Jiang, T
Liang, DC
Issue Date: 2002
Publisher: Blackwell Munksgaard
Source: Acta crystallographica section d - biological crystallography, 2002, v. 58, p. 1479-1481 How to cite?
Journal: Acta Crystallographica Section D-Biological Crystallography 
Abstract: Pyridoxal kinase (ATP:pyridoxal 5'-phosphotransferase; EC 2.7.1.35) is a key enzyme in the transformation of vitamin B-6 to pyridoxal-5'-phosphate. Pyridoxal-5'-phosphate is the crucial cofactor required by numerous enzymes involved in the metabolism of amino acids and the synthesis of many neurotransmitters. Pyridoxal kinase from sheep brain was crystallized in an orthorhombic form using the hanging-drop vapour-diffusion method with sodium citrate as the precipitant. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 59.8, b = 94.4, c = 128.2 Angstrom, and diffract to a resolution of 2.1 Angstrom. Crystals were transferred into a soaking liquid without citrate and two heavy-atom derivatives were prepared.
URI: http://hdl.handle.net/10397/34362
ISSN: 0907-4449
DOI: 10.1107/S0907444902011034
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