4bal | pdb_00004bal

Thaumatin from Thaumatococcus daniellii structure in complex with the europium tris-hydroxymethyltriazoledipicolinate complex at 1.30 A resolution.

spinqualitylabelsall models 4bal, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bal is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.298Å Ligands: EU3, HM6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMed New trisdipicolinic acid-lanthanide complexes are reported as phasing agents for X-ray crystallography of proteins. It is demonstrated that CuAAC modifications allow protein co-crystallization with low concentration of lanthanide complexes leading to an accurate structure determination. Clicked europium dipicolinate complexes for protein X-ray structure determination.,Talon R, Nauton L, Canet JL, Kahn R, Girard E, Gautier A Chem Commun (Camb). 2012 Nov 12;48(97):11886-8. doi: 10.1039/c2cc36982f. PMID:23123834 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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