Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

Citation
K. Min et al., Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A, ACT CRYST D, 56, 2000, pp. 504-505
Citations number
15
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
504 - 505
Database
ISI
SICI code
0907-4449(200004)56:<504:CAPXCA>2.0.ZU;2-B
Abstract
Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and act s as a suppressor of metastasis. It has been crystallized using 2-methyl-2, 4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belongi ng to the space group P2(1), with unit-cell parameters a = 74.21, b = 78.11 , c = 82.29 Angstrom, beta = 101.33 degrees. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V-m) of 2.27 Angstrom(3) Da(-1) and a solvent content of 46%. Native X-ray data to 2.15 Angstrom resolution have been collected using synchrotron X-rays.