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      Protein energy landscapes determined by five-dimensional crystallography

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          Abstract

          Barriers of activation within the photocycle of a photoactive protein were extracted from comprehensive time courses of time resolved crystallographic data collected at multiple temperature settings.

          Abstract

          Free-energy landscapes decisively determine the progress of enzymatically catalyzed reactions [Cornish-Bowden (2012 ), Fundamentals of Enzyme Kinetics, 4th ed.]. Time-resolved macromolecular crystallography unifies transient-state kinetics with structure determination [Moffat (2001 ), Chem. Rev. 101, 1569–1581; Schmidt et al. (2005 ), Methods Mol. Biol. 305, 115–154; Schmidt (2008 ), Ultrashort Laser Pulses in Medicine and Biology] because both can be determined from the same set of X-ray data. Here, it is demonstrated how barriers of activation can be determined solely from five-dimensional crystallo­graphy, where in addition to space and time, temperature is a variable as well [Schmidt et al. (2010 ), Acta Cryst. A 66, 198–206]. Directly linking molecular structures with barriers of activation between them allows insight into the structural nature of the barrier to be gained. Comprehensive time series of crystallo­graphic data at 14 different temperature settings were analyzed and the entropy and enthalpy contributions to the barriers of activation were determined. One hundred years after the discovery of X-ray scattering, these results advance X-ray structure determination to a new frontier: the determination of energy landscapes.

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          Author and article information

          Journal
          Acta Crystallogr D Biol Crystallogr
          Acta Crystallogr. D Biol. Crystallogr
          Acta Cryst. D
          Acta Crystallographica Section D: Biological Crystallography
          International Union of Crystallography
          0907-4449
          1399-0047
          01 December 2013
          19 November 2013
          19 November 2013
          : 69
          : Pt 12 ( publisher-idID: d131200 )
          : 2534-2542
          Affiliations
          [a ]Physics Department, University of Wisconsin-Milwaukee , Milwaukee, Wisconsin, USA
          [b ]Center for Advanced Radiation Sources, The University of Chicago , Chicago, Illinois, USA
          [c ]Center for Nanomaterials and Chemical Reactions, Institute for Basic Science , Daejeon 305-701, Republic of Korea
          [d ]Department of Chemistry, KAIST , Daejeon 305-701, Republic of Korea
          Author notes
          Correspondence e-mail: m-schmidt@ 123456uwm.edu
          Article
          dw5067 ABCRE6 S0907444913025997
          10.1107/S0907444913025997
          3852658
          24311594
          730922dc-056a-463d-b6e6-73d0a23a9184
          © Schmidt et al. 2013

          This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.

          History
          : 26 July 2013
          : 19 September 2013
          Categories
          Research Papers

          photoactive yellow protein,time-resolved microspectrophotometry,five-dimensional crystallography,time-resolved crystallography,chemical kinetics

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