Crystallization and Preliminary X-ray Crystallographic Studies of Phosphoglycerate Kinase from Thermus caldophilus

We report the purification and crystallization of phosphoglycerate kinase from Thermus caldophilus (Tca). The enzyme crystallizes in the P212121 space group (cell dimensions a = 65.1, b = 71.3, c = 80.2 í-), with one molecule in the asymmetric unit. A complete set of diffraction data was collected f...

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Veröffentlicht in:	Molecules and cells 2003, 15(3), , pp.370-372
Hauptverfasser:	Lee, J.H, Im, Y.J, Rho, S.H, Park, S.H, Kang, G.B, Eom, S.H. (Kwangju Institute of Science and Technology, Gwangju, Republic of Korea), Cho, S.J, Kim, T.Y, Shin, H.J, Lee, D.S. (Korea Research Institute of Bioscience and Biothechnology, Daejeon, Korea)
Format:	Artikel
Sprache:	eng
Schlagworte:	CRYSTALLIZATION Crystallization - methods Crystallography, X-Ray - methods Phosphoglycerate Kinase - chemistry Phosphoglycerate Kinase - isolation & purification Thermus - enzymology 생물학
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Zusammenfassung:	We report the purification and crystallization of phosphoglycerate kinase from Thermus caldophilus (Tca). The enzyme crystallizes in the P212121 space group (cell dimensions a = 65.1, b = 71.3, c = 80.2 í-), with one molecule in the asymmetric unit. A complete set of diffraction data was collected from an ortho-rhombic crystal up to 1.8í- resolution.
ISSN:	1016-8478 0219-1032
DOI:	10.1016/S1016-8478(23)13752-6