Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver

Komoto, Junichi; Huang, Yafei; Hu, Yongbo; Takata, Yoshimi; Konishi, Kiyoshi; Ogawa, Hirofumi; Gomi, Tomoharu; Fujioka, Motoji; Takusagawa, Fusao

dc.contributor.author	Komoto, Junichi
dc.contributor.author	Huang, Yafei
dc.contributor.author	Hu, Yongbo
dc.contributor.author	Takata, Yoshimi
dc.contributor.author	Konishi, Kiyoshi
dc.contributor.author	Ogawa, Hirofumi
dc.contributor.author	Gomi, Tomoharu
dc.contributor.author	Fujioka, Motoji
dc.contributor.author	Takusagawa, Fusao
dc.date.accessioned	2015-03-23T20:42:51Z
dc.date.available	2015-03-23T20:42:51Z
dc.date.issued	1999-01-01
dc.identifier.citation	Komoto, Junichi et al. (1999). "Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver." Acta Crystallographica D, 55(11):1928-1929. http://www.dx.doi.org/10.1107/S0907444999010318.	en_US
dc.identifier.issn	0365-110X
dc.identifier.uri	http://hdl.handle.net/1808/17175
dc.description	This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S0907444999010318.	en_US
dc.description.abstract	Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 Å, [beta] = 96.8 (1)° at 93 K, and typically diffract beyond 2.8 Å.	en_US
dc.publisher	International Union of Crystallography	en_US
dc.title	Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver	en_US
dc.type	Article
kusw.kuauthor	Takusagawa, Fusao
kusw.kudepartment	Molecular Biosciences	en_US
dc.identifier.doi	10.1107/S0907444999010318
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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