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dc.contributor.authorBegun, Jake
dc.contributor.authorMcLeish, Michael J.
dc.contributor.authorCaine, Joanne M.
dc.contributor.authorPalant, Elka
dc.contributor.authorGrunewald, Gary L.
dc.contributor.authorMartin, Jennifer L.
dc.date.accessioned2015-05-04T17:36:59Z
dc.date.available2015-05-04T17:36:59Z
dc.date.issued2001
dc.identifier.citationBegun, J., McLeish, M. J., Caine, J. M. Palant, E. Gunewald, and J. L. Martin. "Crystallization of PNMT, the adrenalinesynthesizing enzyme, is critically dependent of a high protein concentration." Acta Cryst. (2002). D58, 314-315 http://dx.doi.org/10.1107/S090744490101962Xen_US
dc.identifier.urihttp://hdl.handle.net/1808/17566
dc.description.abstractPhenylethanolamine N-methyltransferase, PNMT, utilizes the methylating cofactor S-adenosyl-L-methionine to catalyse the synthesis of adrenaline. Human PNMT has been crystallized in complex with an inhibitor and the cofactor product S-adenosyl-L-homocysteine using the hanging-drop technique with PEG 6000 and lithium chloride as precipitant. A critical requirement for crystallization was a high enzyme concentration (>90 mg ml-1) and cryocrystallography was used for high-quality data measurement. Diffraction data measured from a cryocooled crystal extend to a resolution of 2.3 Å. Cryocooled crystals belong to space group P43212 and have unit-cell parameters a = b = 94.3, c = 187.7 Å.en_US
dc.description.sponsorshipWe thank Melissa Edeling and Judy Halliday for technical assistance. JLM is the recipient of an Australian Research Council Senior Research Fellowship. This work was funded by the National Institutes of Health, the Monash Research Fund, the University of Queensland Foundation and the Australian Research Council. The Centre for Functional and Applied Genomics is a Special Research Centre of the Australian Research Council.en_US
dc.publisherInternational Union of Crystallographyen_US
dc.titleCrystallization of PNMT, the adrenalinesynthesizing enzyme, is critically dependent on a high protein concentraitionen_US
dc.typeArticle
kusw.kuauthorGrunewald, Gary L.
kusw.kudepartmentDepartment of Medical Chemistryen_US
dc.identifier.doi10.1107/S090744490101962X
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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