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Crystallization and Preliminary X-ray Diffraction Studies of Curculin
- Source :
- JMB Online (Journal of Molecular Biology); April 28, 1994, Vol. 238 Issue: 2 p286-287, 2p
- Publication Year :
- 1994
-
Abstract
- A taste-modifying protein, curculin, has been crystallized by the vapor diffusion method using polyethylene glycol 400 as a precipitant. The crystals belong to orthorhombic space group P2<SUB>1</SUB>2<SUB>1</SUB>2<SUB>1</SUB> with unit cell dimensions: a=105 Å, b=271 Å, c=48·7 Å. The crystals diffract X-rays to at least a resolution of 3.0 Å and are suitable for X-ray crystallographic studies. Copyright 1994, 1999 Academic Press
Details
- Language :
- English
- ISSN :
- 00222836 and 10898638
- Volume :
- 238
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- JMB Online (Journal of Molecular Biology)
- Publication Type :
- Periodical
- Accession number :
- ejs700212
- Full Text :
- https://doi.org/10.1006/jmbi.1994.1289