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pubmed-article:11807261pubmed:abstractTextPhenylethanolamine 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 A. Cryocooled crystals belong to space group P4(3)2(1)2 and have unit-cell parameters a = b = 94.3, c = 187.7 A.lld:pubmed
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pubmed-article:11807261pubmed:pagination314-5lld:pubmed
pubmed-article:11807261pubmed:dateRevised2007-7-24lld:pubmed
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pubmed-article:11807261pubmed:articleTitleCrystallization of PNMT, the adrenaline-synthesizing enzyme, is critically dependent on a high protein concentration.lld:pubmed
pubmed-article:11807261pubmed:affiliationCentre for Drug Design and Development and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia.lld:pubmed
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pubmed-article:11807261pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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