6FRN
Structure of F420H2 oxidase (FprA) co-crystallized with 10mM Tb-Xo4 and calcium chloride
Summary for 6FRN
| Entry DOI | 10.2210/pdb6frn/pdb |
| Descriptor | F420H2 oxidase (FprA), FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (9 entities in total) |
| Functional Keywords | protein nucleation, phasing, tb-xo4, crystallophore, oxidoreductase |
| Biological source | Methanothermococcus thermolithotrophicus |
| Total number of polymer chains | 4 |
| Total formula weight | 192958.75 |
| Authors | Engilberge, S.,Riobe, F.,Di Pietro, S.,Wagner, T.,Shima, S.,Girard, E.,Dumont, E.,Maury, O. (deposition date: 2018-02-16, 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 (1.74 Å) |
Structure validation
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