1. Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain
- Author
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Chi Kong Lau, Sheng Quan Liu, Tao Jiang, Wenrui Chang, Jiping Zhang, Yun Chung Leung, Minghui Li, Francis Kwok, Dong Cai Liang, and Xiao Min An
- Subjects
chemistry.chemical_classification ,Sheep ,biology ,Protein Conformation ,Stereochemistry ,Brain ,General Medicine ,Metabolism ,Crystallography, X-Ray ,Phosphate ,Pyridoxal kinase ,Cofactor ,Amino acid ,Crystallography ,chemistry.chemical_compound ,Enzyme ,chemistry ,Biochemistry ,Structural Biology ,Sodium citrate ,biology.protein ,Animals ,Crystallization ,Pyridoxal - 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 A, and diffract to a resolution of 2.1 A. Crystals were transferred into a soaking liquid without citrate and two heavy-atom derivatives were prepared.
- Published
- 2002