Preliminary x-ray crystallographic analysis and molecular replacement studies with 2,5-diketo-d-gluconate reductase

Sumit Khurana, David B. Powers, Stephen Anderson, Michael Blaber

Research output: Contribution to journalArticlepeer-review

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 Lascorbic acid. This protein was crystallized in the monoclinic space group P22 with one molecule in the asymmetric unit. The crystals diffract to a maximum resolution of 1.9 Å. An x-ray intensity data set was collected from these crystals and is 85% complete between 60 to 2.1 Å. 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 of 49.2% and a correlation coefficient of 34.0%.

Original languageAmerican English
Pages (from-to)287-290
Number of pages4
JournalProtein and Peptide Letters
Volume4
Issue number4
StatePublished - 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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