4.4 Article

Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain

Journal

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 58, Issue -, Pages 1479-1481

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444902011034

Keywords

-

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available