Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.
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.
Charron
Christophe
C
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.
Kadri
Adel
A
Robert
Marie-Claire
MC
Giegé
Richard
R
Lorber
Bernard
B
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*
D010940:Plant Proteins; D013549:Sweetening Agents; D014867:Water; C003427:thaumatin protein, plant; D005990:Glycerol