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Crystallographic characterization of recombinant human copper zinc superoxide dismutase


Crystallographic characterization of recombinant human copper zinc superoxide dismutase



Journal of Biological Chemistry 261(34): 16215-16218



ISSN/ISBN: 0021-9258

Recombinant human CuZn superoxide dismutase as expressed in yeast has been crystallized in three different crystal forms. Hexagonal plates grow from 2.4 M ammonium sulfate, pH 7.5, and belong to the space group P6322, with cell dimensions a = b = 113.5(3), c = 151.5(5) .ANG., and Vm = 2.21 .ANG.3/dalton for two dimers per asymmetric unit. At 2.0 M ammonium sulfate, pH 7.5, chunky wedges grow in space group C2221, a = 205.2(6), b = 166.5(4), c = 145.4(4) .ANG. with a Vm of 2.43 .ANG.3/dalton for eight dimers per asymmetric unit. With polyethylene glycol 8000, pH7.5-8.0, hexagonal prisms are obtained with cell dimensions a = b = 197.4(6), c = 43.1(2) .ANG., space group P6, and Vm = 2.53 .ANG.3/dalton for three dimers per asymmetric unit. All of these forms diffract to high resolution, are stable to X-rays, and appear suitable for determination of the atomic structure. Crystals of the doubly mutated enzyme (Cys6 .fwdarw. Ala, Cys111 .fwdarw. Ser) grown from both micro- and macroseeds of the wild type protein demonstrate the feasibility of isomorphous crystallization of site-directed mutants of the cloned parent enzyme for comparative structure-function studies.

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Accession: 005072823

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