6RO5
1Yr-Y: Lysozyme with Re Cluster 1 year on shelf
Summary for 6RO5
| Entry DOI | 10.2210/pdb6ro5/pdb |
| Related | 5NBJ |
| Descriptor | Lysozyme C, RHENIUM, CHLORIDE ION, ... (8 entities in total) |
| Functional Keywords | radio-pharmaceuticals, organometallic complex, metal binding protein, antimicrobial protein |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 2 |
| Total formula weight | 36878.32 |
| Authors | Brink, A.,Helliwell, J.R. (deposition date: 2019-05-10, release date: 2019-06-19, Last modification date: 2024-10-16) |
| Primary citation | Brink, A.,Helliwell, J.R. Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging. Iucrj, 6:695-702, 2019 Cited by PubMed Abstract: The fact that a protein crystal can serve as a chemical reaction vessel is intrinsically fascinating. That it can produce an electron-dense tetranuclear rhenium cluster compound from a rhenium tri-carbonyl tri-bromo starting compound adds to the fascination. Such a cluster has been synthesized previously , where it formed under basic conditions. Therefore, its synthesis in a protein crystal grown at pH 4.5 is even more unexpected. The X-ray crystal structures presented here are for the protein hen egg-white lysozyme incubated with a rhenium tri-carbonyl tri-bromo compound for periods of one and two years. These reveal a completed, very well resolved, tetra-rhenium cluster after two years and an intermediate state, where the carbonyl ligands to the rhenium cluster are not yet clearly resolved, after one year. A dense tetranuclear rhenium cluster, and its technetium form, offer enhanced contrast in medical imaging. Stimulated by these crystallography results, the unusual formation of such a species directly in an situation has been considered. It offers a new option for medical imaging compounds, particularly when considering the application of the pre-formed tetranuclear cluster, suggesting that it may be suitable for medical diagnosis because of its stability, preference of formation and biological compatibility. PubMed: 31316813DOI: 10.1107/S2052252519006651 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
Download full validation report
