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dc.contributor.authorShen, Yuequan
dc.contributor.authorTang, Liang
dc.contributor.authorZhou, Hai-Meng
dc.contributor.authorLin, Zheng-jiong
dc.date.accessioned2015-05-05T19:36:17Z
dc.date.available2015-05-05T19:36:17Z
dc.date.issued2001-08-01
dc.identifier.citationShen, Y., Tang, L., Zhou, H., & Lin, Z. (2001). Crystal structure of human muscle creatine kinase. Acta Crystallographica D, 57(8), 1196-1200. http://www.dx.doi.org/10.1107/S0907444901007703en_US
dc.identifier.urihttp://hdl.handle.net/1808/17594
dc.descriptionThis is the publisher's version, also available electronically from "http://scripts.iucr.org".en_US
dc.description.abstractThe crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5 Å resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to occur simultaneously in the crystal. These dimers form an infinite `double-helix'-like structure along an unusual long crystallographic 31 axis.en_US
dc.publisherInternational Union of Crystallographyen_US
dc.subjecthuman muscle creatine kinaseen_US
dc.titleCrystal structure of human muscle creatine kinaseen_US
dc.typeArticle
kusw.kuauthorTang, Liang
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1107/S0907444901007703
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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