title: Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.
abstract: The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced.
authors.affiliation: Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse' UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15Rue René Descartes, F-67084 Strasbourg Cedex, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Charron
authors.forename: Adel
authors.initials: A
authors.lastname: Kadri
authors.forename: Marie-Claire
authors.initials: MC
authors.lastname: Robert
authors.forename: Richard
authors.initials: R
authors.lastname: Giegé
authors.forename: Bernard
authors.initials: B
authors.lastname: Lorber
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005990:Glycerol / Q000737:chemistry*; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D013549:Sweetening Agents / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; D013549:Sweetening Agents; D014867:Water; C003427:thaumatin protein, plant; D005990:Glycerol