Time-resolved x-ray crystallography of heme proteins.

Methods in Enzymology
V Srajer, William E Royer

Abstract

Heme proteins, with their natural photosensitivity, are excellent systems for the application of time-resolved crystallographic methods. Ligand dissociation can be readily initiated by a short laser pulse with global structural changes probed at the atomic level by X-rays in real time. Third-generation synchrotrons provide 100-ps X-ray pulses of sufficient intensity for monitoring very fast processes. Successful application of such time-resolved crystallographic experiments requires that the structural changes being monitored are compatible with the crystal lattice. These techniques have recently permitted observing for the first time allosteric transitions in real time for a cooperative dimeric hemoglobin.

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Citations

Oct 15, 2013·Journal of Synchrotron Radiation·Rita GraceffaThomas C Irving
Jan 23, 2016·Structural Dynamics·M LevantinoM Cammarata
May 15, 2013·Nihon yakurigaku zasshi. Folia pharmacologica Japonica·Atsuko Yamashita
Jul 18, 2016·Biochemistry and Biophysics Reports·Sarah C RozinekLorenzo Brancaleon
Oct 5, 2021·Acta Crystallographica. Section D, Structural Biology·Diana C F MonteiroArwen R Pearson
Sep 29, 2011·Current Opinion in Structural Biology·Moran GrossmanIrit Sagi

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