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Crystallization and preliminary X-ray analysis of brazzein, a new sweet protein
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1996
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X-ray CrystallographyCrystal StructureBioorganic ChemistryMolecular BiologyChemical BiologyProtein RefoldingSweet ProteinProtein FoldingProtein X-ray CrystallographyStructure ElucidationProtein ChemistryBiochemistryNew Sweet ProteinSynchrotron RadiationCrystallographyStructural BiologyNatural SciencesMedicinePreliminary X-ray AnalysisSodium Sulfate
Brazzein is a sweet protein isolated from a wild African plant Pentadiplandra brazzeana. Brazzein is the smallest (molecular mass = 6473 Da) and the most water-soluble protein sweetener discovered so far and is highly thermostable. Crystals were grown by vapor diffusion using sodium sulfate as a precipitant. They belong to the tetragonal space group I4(1)22 with unit-cell parameters a = b = 61.4, c = 59.6 A and with one molecule in the asymmetric unit. The crystals diffract to 1.8 A resolution using synchrotron radiation.