Reference: Badasso MO, et al. (2000) Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae. Acta Crystallogr D Biol Crystallogr 56(Pt 7):915-7

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Abstract


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 and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 A, 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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Badasso MO, Read JA, Dhanaraj V, Cooper JB, Wood SP, Blundell TL, Dreyer T, Winther J
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