1kwn
From Proteopedia
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| - | [[Image:1kwn.jpg|left|200px]] | + | [[Image:1kwn.jpg|left|200px]] |
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| - | '''1.2 A Structure of Thaumatin Crystallized in Gel''' | + | {{Structure |
| + | |PDB= 1kwn |SIZE=350|CAPTION= <scene name='initialview01'>1kwn</scene>, resolution 1.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=TAR:D(-)-TARTARIC ACID'>TAR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''1.2 A Structure of Thaumatin Crystallized in Gel''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KWN is a [ | + | 1KWN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12112683 12112683] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
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[[Category: sweet tasting protein]] | [[Category: sweet tasting protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:23:17 2008'' |
Revision as of 10:23, 20 March 2008
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| , resolution 1.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 12:23:17 2008
