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Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae by M. O. Badasso; J. A. Read; V. Dhanaraj; J. B. Cooper; S. P. Wood; T. L. Blundell; T. Dreyer; J. Winther is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae about?
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor I A 3, found in the cytosol. The I A 3±saccharopepsin complex crystals belong to the space group P6 2 22, with unit-cell parameters a = b = 192.1, c = 59.80 A Ê and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 A Ê , similar to native saccharopepsin crystals. This is probably a consequence in part of glycosylation of the native saccharopepsin. Full structural analysis of the complex crystal is in progress.
Who reads Purification, co-crystallization and preliminary X-ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- M. O. Badasso; J. A. Read; V. Dhanaraj; J. B. Cooper; S. P. Wood; T. L. Blundell; T. Dreyer; J. Winther
- Publisher
- International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)
- Published
- 2000
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)