Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain

Ming Hui Li, Francis Kwok, Xiao Min An, Wen Rui Chang, Chi Kong Lau, Ji Ping Zhang, Sheng Quan Liu, Yun Chung Leung, Tao Jiang, Dong Cai Liang

Research output: Journal article publicationJournal articleAcademic researchpeer-review

6 Citations (Scopus)

Abstract

Pyridoxal kinase (ATP:pyridoxal 5′-phosphotransferase; EC 2.7.1.35) is a key enzyme in the transformation of vitamin B6 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 P212121, with unit-cell parameters a = 59.8, b = 94.4, c = 128.2 Å, and diffract to a resolution of 2.1 Å. Crystals were transferred into a soaking liquid without citrate and two heavy-atom derivatives were prepared.
Original languageEnglish
Pages (from-to)1479-1481
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number9
DOIs
Publication statusPublished - 1 Sep 2002
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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