1IO5

HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTION

Summary for 1IO5

Entry DOI	10.2210/pdb1io5/pdb
Descriptor	LYSOZYME C (2 entities in total)
Functional Keywords	hydrogen, hydration, hydrolase
Biological source	Gallus gallus (chicken)
Cellular location	Secreted: P00698
Total number of polymer chains	1
Total formula weight	14331.16
Authors	Niimura, N.,Minezaki, Y.,Nonaka, T.,Castagna, J.C.,Cipriani, F.,Hoeghoej, P.,Lehmann, M.S.,Wilkinson, C. (deposition date: 2001-01-14, release date: 2001-02-07, Last modification date: 2024-10-16)
Primary citation	Niimura, N.,Minezaki, Y.,Nonaka, T.,Castagna, J.C.,Cipriani, F.,Hoghoj, P.,Lehmann, M.S.,Wilkinson, C. Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography. Nat.Struct.Biol., 4:909-914, 1997 Cited by PubMed Abstract: Neutron quasi-Laue diffraction data (2 A resolution) from tetragonal hen egg-white lysozyme were collected in ten days with neutron imaging plates. The data processing Laue software, LAUEGEN, developed for X-ray Laue diffractometry, was adapted for neutron diffractometry with a cylindrical detector. The data analysis software, X-PLOR, was modified and used for the refinement of hydrogen atoms, and the positions of 960 hydrogen atoms in the protein and 157 bound water molecules, were determined. Several examples are given of the methods used to identify hydrogen atoms and water molecules. PubMed: 9360606 DOI: 10.1038/nsb1197-909 PDB entries with the same primary citation
Experimental method	NEUTRON DIFFRACTION (2 Å)

Structure validation