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6FRO

Crystal structure of Hen Egg-White Lysozyme co-crystallized in presence of 100 mM Tb-Xo4 and 100 mM potassium iodide.

Summary for 6FRO
Entry DOI10.2210/pdb6fro/pdb
DescriptorLysozyme C, TERBIUM(III) ION, IODIDE ION, ... (6 entities in total)
Functional Keywordsnucleation, phasing, tb-xo4, crystallophore, hydrolase
Biological sourceGallus gallus (Chicken)
Total number of polymer chains1
Total formula weight15703.95
Authors
Engilberge, S.,Riobe, F.,Di Pietro, S.,Girard, E.,Dumont, E.,Maury, O. (deposition date: 2018-02-16, release date: 2018-10-03, Last modification date: 2024-01-17)
Primary citationEngilberge, 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: 29806881
DOI: 10.1002/chem.201802172
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.42 Å)
Structure validation

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