6F2M
Structure of the bacteriophage T5 distal tail protein pb9 co-crystallized with 10mM Tb-Xo4
Summary for 6F2M
| Entry DOI | 10.2210/pdb6f2m/pdb |
| Descriptor | Distal tail protein, Tb-Xo4, 1,2-ETHANEDIOL, ... (7 entities in total) |
| Functional Keywords | phage protein, crystallophore, tb-xo4, nucleation, phasing, lanthanide complexes, viral protein |
| Biological source | Escherichia phage T5 (Enterobacteria phage T5) |
| Total number of polymer chains | 4 |
| Total formula weight | 100149.26 |
| Authors | Engilberge, S.,Riobe, F.,Di Pietro, S.,Breyton, C.,Girard, E.,Dumont, E.,Maury, O. (deposition date: 2017-11-24, release date: 2018-10-03, Last modification date: 2024-05-08) |
| Primary citation | Engilberge, S.,Riobe, F.,Wagner, T.,Di Pietro, S.,Breyton, C.,Franzetti, B.,Shima, S.,Girard, E.,Dumont, E.,Maury, O. Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography. Chemistry, 24:9739-9746, 2018 Cited by PubMed Abstract: 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. PubMed: 29806881DOI: 10.1002/chem.201802172 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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