Crystallization of native and selenomethionyl yeast orotidine 5 '-phosphate decarboxylase

Citation
Bg. Miller et al., Crystallization of native and selenomethionyl yeast orotidine 5 '-phosphate decarboxylase, ACT CRYST D, 56, 2000, pp. 472-474
Citations number
16
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
4
Pages
472 - 474
Database
ISI
SICI code
0907-4449(200004)56:<472:CONASY>2.0.ZU;2-8
Abstract
Crystals of the Saccharomyces cerevisiae pyrimidine biosynthetic enzyme oro tidine 5'-phosphate decarboxylase (ODCase) were grown by the hanging-drop v apor-diffusion technique at 277 K using polyethylene glycol 4000 as the pre cipitant. Crystals of native and selenomethionyl ODCase diffract to less th an 2.2 Angstrom and belong to the orthorhombic space group P2(1)2(1)2(1), w ith unit-cell parameters a = 90.1, b = 116.2, c = 117.0 Angstrom. Crystals of ODCase grown in the presence of the postulated transition-state analog i nhibitor 6-hydroxyuridine 5'-phosphate (BMP) diffract to less than 2.5 Angs trom and belong to space group P2(1), with unit-cell parameters a = 79.9, b = 80.0, c = 98.2 Angstrom, beta = 108.6 degrees.