C.Charron
et al.
(2004).
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.
Acta Crystallogr D Biol Crystallogr,
60,
83-89.
PubMed id: 14684896
DOI: 10.1107/S0907444903022613
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.
C.Charron,
R.Giegé,
B.Lorber.
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.
Literature references that cite this PDB file's key reference
R.Kant
(2005).
Sweet proteins--potential replacement for artificial low calorie sweeteners.
Nutr J, 4,
5.
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