1pp3
Structure of thaumatin in a hexagonal space group
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OverviewOverview
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.
About this StructureAbout this Structure
1PP3 is a Single protein structure of sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA.
ReferenceReference
Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices., Charron C, Giege R, Lorber B, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):83-9. Epub 2003 Dec, 18. PMID:14684896
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