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

dc.contributor.authorKomoto, Junichi
dc.contributor.authorHuang, Yafei
dc.contributor.authorHu, Yongbo
dc.contributor.authorTakata, Yoshimi
dc.contributor.authorKonishi, Kiyoshi
dc.contributor.authorOgawa, Hirofumi
dc.contributor.authorGomi, Tomoharu
dc.contributor.authorFujioka, Motoji
dc.contributor.authorTakusagawa, Fusao
dc.date.accessioned2015-03-23T20:42:51Z
dc.date.available2015-03-23T20:42:51Z
dc.date.issued1999-01-01
dc.identifier.citationKomoto, 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.issn0365-110X
dc.identifier.urihttp://hdl.handle.net/1808/17175
dc.descriptionThis is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S0907444999010318.en_US
dc.description.abstractGuanidinoacetate 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.publisherInternational Union of Crystallographyen_US
dc.titleCrystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liveren_US
dc.typeArticle
kusw.kuauthorTakusagawa, Fusao
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1107/S0907444999010318
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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