1LY0

Structure of thaumatin crystallized in the presence of glycerol

Summary for 1LY0

• Entry DOI: 10.2210/pdb1ly0/pdb
• Related: 1LXZ
• Descriptor: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: taste-modifying protein, sweet protein, plant protein
• Biological source: Thaumatococcus daniellii (miracle fruit)
• Cellular location: Cytoplasmic vesicle: P02883
• Total number of polymer chains: 1
• Total formula weight: 22377.15

Authors

Charron, C.,Kadri, A.,Robert, M.C.,Giege, R.,Lorber, B. (deposition date: 2002-06-06, release date: 2003-01-14, Last modification date: 2024-11-20)

Primary citation

Charron, C.,Kadri, A.,Robert, M.C.,Giege, R.,Lorber, B.
Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.
Acta Crystallogr.,Sect.D, 58:2060-2065, 2002

PubMed 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.

PubMed: 12454465
DOI: 10.1107/S0907444902017183

Experimental method

X-RAY DIFFRACTION (1.36 Å)