International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

© International Union of Crystallography 2006
International Tables for Crystallography (2006). Vol. F. ch. 8.2, p. 171

Table 8.2.5.1 

K. Moffata*

aDepartment of Biochemistry and Molecular Biology, The Center for Advanced Radiation Sources, and The Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA
Correspondence e-mail: moffat@cars.uchicago.edu

Table 8.2.5.1 | top | pdf |
Time-resolved Laue diffraction experiments

This table is adapted from Table 2 of Ren et al. (1999)[link], in which citations of the original experiments are provided.

Protein Time resolution Experiment
Hen lysozyme 64 ms Temperature jump test
Glycogen phosphorylase 1 s Bound maltoheptose
Hen lysozyme 1 s Radiation damage test
Glycogen phosphorylase 100 ms Use of caged phosphate
Ras oncogene product 1 s GTP complex
γ-Chymotrypsin 5 s Photolysis of cinnamate/pyrone
Trypsin 800 ms Ordered hydrolytic water
Cytochrome c peroxidase 1 s Redox active compound I
Hen lysozyme 10 ms Temperature jump
Isocitrate dehydrogenase 50 ms ES complex and intermediate
Isocitrate dehydrogenase 10 ms Product complex
Photoactive yellow protein 10 ms pB-like intermediate
Photoactive yellow protein 10 ns pR-like intermediate
CO-myoglobin 10 ns Photolyzed CO species at 290 K
CO-myoglobin 8 ms Photolyzed CO species at 20–40 K
Hydroxymethylbilane synthase 1.5 ms Mutant enzyme–cofactor complex