6f2m

Structure of the bacteriophage T5 distal tail protein pb9 co-crystallized with 10mM Tb-Xo4

spinqualitylabelsall models 6f2m, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f2m is a 4 chain structure with sequence from Escherichia virus T5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: 7MT, CL, EDO, NA, TB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DIT_BPT5 Distal tail protein which forms a hexameric ring located at the tail tube end. Publication Abstract from PubMed Crystallophores are lanthanide complexes that act as powerful auxiliary for protein crystallography due to their strong nucleating and phasing effects. To get first insights on the mechanisms behind nucleation induced by Crystallophore, we systematically identified various elaborated networks of supramolecular interactions between Tb-Xo4 and subset of 6 protein structures determined by X-ray diffraction in complex with terbium-Crystallophore (Tb-Xo4). Such interaction mapping analyses demonstrate the versatile binding behavior of the Crystallophore and pave the way to a better understanding of its unique properties. Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography.,Engilberge S, Riobe F, Wagner T, Di Pietro S, Breyton C, Franzetti B, Shima S, Girard E, Dumont E, Maury O Chemistry. 2018 Jul 11;24(39):9739-9746. doi: 10.1002/chem.201802172. Epub 2018, Jun 25. PMID:29806881 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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