Crystallization and preliminary crystallographic study of cathepsin D inhibitor from potatoes

M Baudys; M Ghosh; K Harlos; M Mares; M Fusek; V Kostka; C C Blake

doi:10.1016/0022-2836(91)90869-8

Crystallization and preliminary crystallographic study of cathepsin D inhibitor from potatoes

J Mol Biol. 1991 Mar 5;218(1):21-2. doi: 10.1016/0022-2836(91)90869-8.

Authors

M Baudys¹, M Ghosh, K Harlos, M Mares, M Fusek, V Kostka, C C Blake

Affiliation

¹ Laboratory of Molecular Biophysics, University of Oxford, U.K.

PMID: 2002505
DOI: 10.1016/0022-2836(91)90869-8

Abstract

Single crystals of the glycosylated inhibitor of cathepsin D and trypsin isolated from potato tubers were obtained using the hanging drop vapor diffusion method and ammonium nitrate as precipitant. The crystals exhibit strong F222 pseudo symmetry but belong to the orthorhombic space group C222 or C222(1), with cell parameters a = 73.8 A, b = 119.9 A and c = 133.2 A with two molecules per asymmetric unit. The crystals diffract to a resolution of 2.4 A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cathepsin D / antagonists & inhibitors*
Crystallization
Freeze Drying
Plant Proteins*
Protein Conformation
Proteins / chemistry*
Proteins / isolation & purification
Solanum tuberosum*
X-Ray Diffraction

Substances

Plant Proteins
Proteins
CDI protein, Solanum tuberosum
Cathepsin D