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Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain. | LitMetric

Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain.

Acta Crystallogr D Biol Crystallogr

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, People's Republic of China.

Published: September 2002

AI Article Synopsis

  • Pyridoxal kinase is an important enzyme that converts vitamin B(6) to its active form, pyridoxal-5'-phosphate, which is essential for amino acid metabolism and neurotransmitter synthesis.
  • The enzyme was successfully crystallized from sheep brain using the hanging-drop vapor-diffusion technique and sodium citrate as a precipitant.
  • The resulting crystals are of high quality, belonging to a specific space group and capable of diffracting at a resolution of 2.1 A, and were further treated to prepare heavy-atom derivatives for analysis.

Article 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.

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Source
http://dx.doi.org/10.1107/S0907444902011034DOI Listing

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