Room-temperature ultrahigh-resolution time-of-flight neutron and X-ray diffraction studies of H/D-exchanged crambin.
The room-temperature (RT) X-ray structure of H/D-exchanged crambin is reported at 0.85 Å resolution. As one of the very few proteins refined with anisotropic atomic displacement parameters at two temperatures, the dynamics of atoms in the RT and 100 K structures are compared. Neutron diffraction data from an H/D-exchanged crambin crystal collected at the Protein Crystallography Station (PCS) showed diffraction beyond 1.1 Å resolution. This is the highest resolution neutron diffraction reported to date for a protein crystal and will reveal important details of the anisotropic motions of H and D atoms in protein structures.
Institute of Biophysical Chemistry, Goethe University Frankfurt, Frankfurt, Germany. chen@chemie.uni-frankfurt.de
Julian C-H
JC
Chen
Zoë
Z
Fisher
Andrey Y
AY
Kovalevsky
Marat
M
Mustyakimov
B Leif
BL
Hanson
Vladimir V
VV
Zhurov
Paul
P
Langan
D018360:Crystallography, X-Ray / Q000379:methods*; D008958:Models, Molecular; D033363:Neutron Diffraction / Q000379:methods*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D013696:Temperature; D013997:Time Factors
D011506:Proteins