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

Abstract

Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts 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, belonging to the space group P2(1), with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 A, beta = 101. 33 degrees. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 A(3) Da(-1) and a solvent content of 46%. Native X-ray data to 2.15 A resolution have been collected using synchrotron X-rays.

• Authors: K Min, S Y Kim, H K Song, C Chang, S J Cho, J Moon, J K Yang, J Y Lee, K J Lee, S W Suh
• Journal: Acta crystallographica. Section D, Biological crystallography (Acta Crystallogr D Biol Crystallogr) Vol. 56 Issue Pt 4 Pg. 503-4 (Apr 2000) ISSN: 0907-4449 [Print] United States
• PMID: 10739934 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Macromolecular Substances
• Recombinant Proteins
• Nucleoside-Diphosphate Kinase

Topics

• Crystallization
• Crystallography, X-Ray
• Humans
• Macromolecular Substances
• Nucleoside-Diphosphate Kinase (chemistry, isolation & purification)
• Recombinant Proteins (chemistry, isolation & purification)