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Science 6 December 1996:
Vol. 274. no. 5293, pp. 1726 - 1729
DOI: 10.1126/science.274.5293.1726
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Reports

Photolysis of the Carbon Monoxide Complex of Myoglobin: Nanosecond Time-Resolved Crystallography

Vukica Srajer, Tsu-yi Teng, Thomas Ursby, Claude Pradervand, Zhong Ren, Shin-ichi Adachi, Wilfried Schildkamp, Dominique Bourgeois, Michael Wulff, Keith Moffat *

The biological activity of macromolecules is accompanied by rapid structural changes. The photosensitivity of the carbon monoxide complex of myoglobin was used at the European Synchrotron Radiation Facility to obtain pulsed, Laue x-ray diffraction data with nanosecond time resolution during the process of heme and protein relaxation after carbon monoxide photodissociation and during rebinding. These time-resolved experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale.

V. Srajer, T.-y. Teng, C. Pradervand, Z. Ren, W. Schildkamp, K. Moffat, Department of Biochemistry and Molecular Biology and the Consortium for Advanced Radiation Sources, The University of Chicago, Chicago, IL 60637, USA.
T. Ursby and M. Wulff, European Synchrotron Radiation Facility (ESRF), 38043 Grenoble Cedex, France.
S.-i. Adachi, Biophysical Chemistry Laboratory, Institute of Physical and Chemical Research, Saitama 351-01, Japan.
D. Bourgeois, UPR 9015/IBS, 38027 Grenoble, France, and ESRF, 38043 Grenoble Cedex, France.
*   To whom correspondence should be addressed.

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