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Crystallization of PNMT, the adrenalinesynthesizing enzyme, is critically dependent on a high protein concentraition
Begun, Jake McLeish, Michael J. Caine, Joanne M. Palant, Elka Grunewald, Gary L. Martin, Jennifer L.
Begun, Jake
McLeish, Michael J.
Caine, Joanne M.
Palant, Elka
Grunewald, Gary L.
Martin, Jennifer L.
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Abstract
Phenylethanolamine 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.
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2001
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International Union of Crystallography
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Begun, 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/S090744490101962X