Crystallization and Preliminary X-Ray Analysis of Human Muscle Creatine Kinase

Tang, Liang; Zhou, Hai-Meng; Lin, Zheng-jiong

dc.contributor.author	Tang, Liang
dc.contributor.author	Zhou, Hai-Meng
dc.contributor.author	Lin, Zheng-jiong
dc.date.accessioned	2015-05-05T19:16:12Z
dc.date.available	2015-05-05T19:16:12Z
dc.date.issued	1999-03-01
dc.identifier.citation	Tang, L., Zhou, H., & Lin, Z. (1999). Crystallization and preliminary X-ray analysis of human muscle creatine kinase. Acta Crystallographica Section D Biological Crystallography, 55(3), 669-670. http://www.dx.doi.org/10.1107/S0907444998011044	en_US
dc.identifier.uri	http://hdl.handle.net/1808/17592
dc.description	This is the publisher's version, also available electronically from "http://scripts.iucr.org".	en_US
dc.description.abstract	Creatine kinase is a key enzyme in the energy homeostasis of cells and tissues with high and fluctuating energy demands. Human muscle MM creatine kinase is a dimeric protein with a molecular weight of \sim43 kDa for each subunit. It has been crystallized by the hanging-drop vapor-diffusion method using 2-methyl-2,4-pentanediol as precipitant. The crystals belong to the enantiomorphous space group P6_222 or P6_422 with cell parameters of a=b=89.11 and c=403.97 Å. The asymmetric unit of the crystal contains two subunits. A data set at 3.3 Å resolution has been collected using synchrotron radiation.	en_US
dc.publisher	International Union of Crystallography	en_US
dc.subject	creatine kinase	en_US
dc.subject	synchrotron radiation	en_US
dc.title	Crystallization and Preliminary X-Ray Analysis of Human Muscle Creatine Kinase	en_US
dc.type	Article
kusw.kuauthor	Tang, Liang
kusw.kudepartment	Molecular Biosciences	en_US
kusw.oanotes	Per SHERPA/RoMEO 5/5/2015: On author's personal website, employer's website, employer's repository, or subject-based repository. Publisher's version/PDF may be used (authorised electronic re-print) (preferred). Publisher's version/PDF (authorised electronic re-print) on PubMed Central and related servers. Pre-print must acknowledge submission to journal. Must link to publisher version on IUCr server. Published source must be acknowledged with citation. Publisher last contacted on 23/04/2014	en_US
dc.identifier.doi	10.1107/S0907444998011044
kusw.oaversion	Scholarly/refereed, publisher version
kusw.oapolicy	This item does not meet KU Open Access policy criteria.
dc.rights.accessrights	openAccess

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