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

Title
Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A
Authors
Min K.Kim S.Y.Song H.K.Chang C.Cho S.-J.Moon J.Yang J.K.Lee J.Y.Lee K.-J.Suh S.W.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2000
Journal Title
Acta Crystallographica Section D: Biological Crystallography
ISSN
0907-4449JCR Link
Citation
vol. 56, no. 4, pp. 504 - 505
Indexed
SCOPUS WOS scopus
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 P21, with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 Å, β = 101.33°. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 Å3 Da-1 and a solvent content of 46%. Native X-ray data to 2.15 Å resolution have been collected using synchrotron X-rays.
DOI
10.1107/S0907444900002626
Appears in Collections:
약학대학 > 약학과 > Journal papers
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