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2004
Charron C, Giege R, Lorber B
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices Journal Article
In: Acta Crystallogr D Biol Crystallogr, vol. 60, no. Pt 1, pp. 83-89, 2004, ISBN: 14684896, (0907-4449 Journal Article).
Abstract | Links | BibTeX | Tags: GIEGE Comparative Study Crystallization Crystallography, Molecular Plant Proteins/*chemistry Support, Non-U.S. Gov't, Unité ARN, X-Ray Hydrogen Bonding Models
@article{,
title = {Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices},
author = {C Charron and R Giege and B Lorber},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14684896},
isbn = {14684896},
year = {2004},
date = {2004-01-01},
journal = {Acta Crystallogr D Biol Crystallogr},
volume = {60},
number = {Pt 1},
pages = {83-89},
abstract = {The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.},
note = {0907-4449
Journal Article},
keywords = {GIEGE Comparative Study Crystallization Crystallography, Molecular Plant Proteins/*chemistry Support, Non-U.S. Gov't, Unité ARN, X-Ray Hydrogen Bonding Models},
pubstate = {published},
tppubtype = {article}
}
The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.
2002
Sauter C, Lorber B, Giege R
Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature Journal Article
In: Proteins, vol. 48, no. 2, pp. 146-150, 2002, ISBN: 12112683, (1097-0134 Journal Article).
Abstract | Links | BibTeX | Tags: Crystallization *Crystallography, FRUGIER, Molecular Plant Proteins/*chemistry Support, Non-U.S. Gov't *Sweetening Agents Temperature Weightlessness, SAUTER, Unité ARN, X-Ray Hydrogels/*chemistry *Models
@article{,
title = {Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature},
author = {C Sauter and B Lorber and R Giege},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12112683},
isbn = {12112683},
year = {2002},
date = {2002-01-01},
journal = {Proteins},
volume = {48},
number = {2},
pages = {146-150},
abstract = {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.},
note = {1097-0134
Journal Article},
keywords = {Crystallization *Crystallography, FRUGIER, Molecular Plant Proteins/*chemistry Support, Non-U.S. Gov't *Sweetening Agents Temperature Weightlessness, SAUTER, Unité ARN, X-Ray Hydrogels/*chemistry *Models},
pubstate = {published},
tppubtype = {article}
}
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.