Abstract
Abstract: 2,5 diketo-D-gluconate reductase (2,5-DKG reductase) is an enzyme with considerable commercial interest because it can be used to manufacture 2-keto-L-gulonic acid, a key intermediate in the industrial synthesis of L ascorbic acid. This protein was crystallized in the monoclinic space group P21 with one molecule in the asymmetric unit. The crystals diffract to a maximum resolution of 1.9 A. An x-ray intensity data set was collected from these crystals and is 85% complete between 60 to 2.1 A. An initial structure solution has been attempted using the molecular replacement method with human aldose reductase (38% sequence identity) as a search model. The rotation and translation function searches yield a single clear peak above the background noise level with a corresponding R factor of49.2% and a correlation coefficient of34.0%.
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