9GHX

Lysozyme covalently bound to fac-[Re(CO)3-imidazole] complex, incubated for 112 weeks. Data collection done at mammalian body temperature.

Summary for 9GHX

Entry DOI	10.2210/pdb9ghx/pdb
Descriptor	Lysozyme C, CHLORIDE ION, Tricarbonyl di(imidazole) rhenium(I), ... (8 entities in total)
Functional Keywords	c-type lysozyme, lysozyme-like fold, glycoside hydrolase, rhenium tricarbonyl, antimicrobial protein
Biological source	Gallus gallus (chicken)
Total number of polymer chains	1
Total formula weight	16102.54
Authors	Jacobs, F.J.F.,Brink, A.,Helliwell, J.R. (deposition date: 2024-08-16, release date: 2024-10-16, Last modification date: 2024-12-04)
Primary citation	Jacobs, F.J.F.,Helliwell, J.R.,Brink, A. Body temperature protein X-ray crystallography at 37 °C: a rhenium protein complex seeking a physiological condition structure. Chem.Commun.(Camb.), 60:14030-14033, 2024 Cited by PubMed Abstract: The retention of the covalent binding of an organometalllic rhenium complex as a model for a technetium-99m imaging agent, to a protein at physiological body temperature 37 °C is described. Detailed structure comparisons are made to the related 100 K crystal structure. The generality of the need for this sort of analytical procedure for guiding ligand lead compound discovery is emphasised. PubMed: 39382205 DOI: 10.1039/d4cc04245j PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.19 Å)

Structure validation