1kwn
From Proteopedia
|
1.2 A Structure of Thaumatin Crystallized in Gel
Overview
One reason for introducing a gel in the crystallization medium of proteins, is its ability to reduce convection in solution. This can lead to better, nucleation and growth conditions, and to crystals having enhanced, diffraction properties. We report here the X-ray characterization at room, temperature of high-quality crystals of the intensely sweet thaumatin, prepared in a sodium tartrate solution gelified with 0.15% (m/v) agarose., Using a synchrotron radiation, these crystals diffracted to a previously, unachieved resolution. A diffraction dataset was collected from four, crystals at a resolution of 1.2 A with a R(sym) of 3.6% and a completeness, of 99%. Refinement was carried out to a final crystallographic R-factor of, 12.0%. The quality of the electron density map allowed for the observation, of fine structural details in the protein and its solvation shell., Crystallization in gel might be used more generally to improve the quality, of macromolecular crystals. Advantages provided by the gelified medium in, the frame of structural studies are emphasized.
About this Structure
1KWN is a Single protein structure of sequence from Thaumatococcus daniellii with TAR as ligand. Full crystallographic information is available from OCA.
Reference
Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature., Sauter C, Lorber B, Giege R, Proteins. 2002 Aug 1;48(2):146-50. PMID:12112683
Page seeded by OCA on Tue Nov 20 20:01:35 2007
