Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.
Identifieur interne : 000479 ( Main/Exploration ); précédent : 000478; suivant : 000480Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.
Auteurs : Claude Sauter [France] ; Bernard Lorber ; Richard GiegéSource :
- Proteins [ 1097-0134 ] ; 2002.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Hydrogels, Protéines végétales.
- Cristallisation, Cristallographie aux rayons X, Impesanteur, Modèles moléculaires, Température, Édulcorants.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Hydrogels, Plant Proteins.
- Crystallization, Crystallography, X-Ray, Models, Molecular, Sweetening Agents, Temperature, Weightlessness.
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.
DOI: 10.1002/prot.10125
PubMed: 12112683
Affiliations:
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12112683</PMID><DateCompleted><Year>2002</Year><Month>09</Month><Day>23</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>48</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Aug</Month><Day>01</Day></PubDate></JournalIssue><Title>Proteins</Title><ISOAbbreviation>Proteins</ISOAbbreviation></Journal><ArticleTitle>Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.</ArticleTitle><Pagination><MedlinePgn>146-50</MedlinePgn></Pagination><Abstract><AbstractText>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. 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