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.
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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)
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Chemical References |
- Macromolecular Substances
- Recombinant Proteins
- Nucleoside-Diphosphate Kinase
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Topics |
- Crystallization
- Crystallography, X-Ray
- Humans
- Macromolecular Substances
- Nucleoside-Diphosphate Kinase
(chemistry, isolation & purification)
- Recombinant Proteins
(chemistry, isolation & purification)
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