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

International Tables for Crystallography (2006). Vol. F, ch. 8.2, p. 171   | 1 | 2 |

Section 8.2.5. Conclusions

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:

8.2.5. Conclusions

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Only a small number of biochemical systems have been subjected to time-resolved crystallographic analysis (Table;[link] Ren et al., 1999[link]). The experiments are technically demanding, require careful planning in the execution, in data analysis and in data interpretation, and strategies for the evaluation of mechanism are still being developed. However, road maps exist for several successful classes of experiments (see e.g. Stoddard et al., 1998[link]; Moffat, 1998[link]; Ren et al., 1999[link]) and new biological systems to which such analyses may be readily applied are being developed. In a world of structural genomics where structures themselves are ten-a-penny, a structure-based understanding of mechanism at the chemical level is still rare. The contributions of crystallography to functional – not merely structural – genomics may be large indeed.

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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.

ProteinTime resolutionExperiment
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


Moffat, K. (1997). Laue diffraction. Methods Enzymol. 277B, 433–447.
Moffat, K. (1998). Ultrafast time-resolved crystallography. Nature Struct. Biol. 5, 641–643.
Ren, Z., Bourgeois, D., Helliwell, J. R., Moffat, K., Šrajer, V. & Stoddard, B. L. (1999). Laue crystallography: coming of age. J. Synchrotron Rad. 6, 891–917.
Stoddard, B. L., Cohen, B. E., Brubaker, M., Mesecar, A. D. & Koshland, D. E. Jr (1998). Millisecond Laue structures of an enzyme-product complex using photocaged substrate analogues. Nature Struct. Biol. 5, 891–897.

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