Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography.
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.
Niimura
N
N
Advanced Science Research Center, Japan Atomic Energy Research Institute, Tokai-mura, Japan. niimura@kotai3.tokai.jaeri.go.jp
Minezaki
Y
Y
Nonaka
T
T
Castagna
J C
JC
Cipriani
F
F
Høghøj
P
P
Lehmann
M S
MS
Wilkinson
C
C
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003461:Crystallography / Q000295:instrumentation / Q000379:methods*; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D009502:Neutrons; D017434:Protein Structure, Tertiary; D012984:Software; D014867:Water / Q000737:chemistry
D014867:Water; D009113:Muramidase