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dc.contributor.authorTang, Liang
dc.contributor.authorZhou, Hai-Meng
dc.contributor.authorLin, Zheng-jiong
dc.date.accessioned2015-05-05T19:16:12Z
dc.date.available2015-05-05T19:16:12Z
dc.date.issued1999-03-01
dc.identifier.citationTang, 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/S0907444998011044en_US
dc.identifier.urihttp://hdl.handle.net/1808/17592
dc.descriptionThis is the publisher's version, also available electronically from "http://scripts.iucr.org".en_US
dc.description.abstractCreatine 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.publisherInternational Union of Crystallographyen_US
dc.subjectcreatine kinaseen_US
dc.subjectsynchrotron radiationen_US
dc.titleCrystallization and Preliminary X-Ray Analysis of Human Muscle Creatine Kinaseen_US
dc.typeArticle
kusw.kuauthorTang, Liang
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1107/S0907444998011044
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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