ALBERT

Description: Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.

Description: Single-particle structure determination by correlations of snapshot X-ray diffraction patterns Nature Communications 3, 1276 (2012). doi:10.1038/ncomms2288 Authors: D. Starodub, A. Aquila, S. Bajt, M. Barthelmess, A. Barty, C. Bostedt, J.D. Bozek, N. Coppola, R.B. Doak, S.W. Epp, B. Erk, L. Foucar, L. Gumprecht, C.Y. Hampton, A. Hartmann, R. Hartmann, P. Holl, S. Kassemeyer, N. Kimmel, H. Laksmono, M. Liang, N.D. Loh, L. Lomb, A.V. Martin, K. Nass, C. Reich, D. Rolles, B. Rudek, A. Rudenko, J. Schulz, R.L. Shoeman, R.G. Sierra, H. Soltau, J. Steinbrener, F. Stellato, S. Stern, G. Weidenspointner, M. Frank, J. Ullrich, L. Strüder, I. Schlichting, H.N. Chapman, J.C.H. Spence & M.J. Bogan

Description: X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction 'snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals ( approximately 200 nm to 2 mum in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3429598/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3429598/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Henry N -- Fromme, Petra -- Barty, Anton -- White, Thomas A -- Kirian, Richard A -- Aquila, Andrew -- Hunter, Mark S -- Schulz, Joachim -- DePonte, Daniel P -- Weierstall, Uwe -- Doak, R Bruce -- Maia, Filipe R N C -- Martin, Andrew V -- Schlichting, Ilme -- Lomb, Lukas -- Coppola, Nicola -- Shoeman, Robert L -- Epp, Sascha W -- Hartmann, Robert -- Rolles, Daniel -- Rudenko, Artem -- Foucar, Lutz -- Kimmel, Nils -- Weidenspointner, Georg -- Holl, Peter -- Liang, Mengning -- Barthelmess, Miriam -- Caleman, Carl -- Boutet, Sebastien -- Bogan, Michael J -- Krzywinski, Jacek -- Bostedt, Christoph -- Bajt, Sasa -- Gumprecht, Lars -- Rudek, Benedikt -- Erk, Benjamin -- Schmidt, Carlo -- Homke, Andre -- Reich, Christian -- Pietschner, Daniel -- Struder, Lothar -- Hauser, Gunter -- Gorke, Hubert -- Ullrich, Joachim -- Herrmann, Sven -- Schaller, Gerhard -- Schopper, Florian -- Soltau, Heike -- Kuhnel, Kai-Uwe -- Messerschmidt, Marc -- Bozek, John D -- Hau-Riege, Stefan P -- Frank, Matthias -- Hampton, Christina Y -- Sierra, Raymond G -- Starodub, Dmitri -- Williams, Garth J -- Hajdu, Janos -- Timneanu, Nicusor -- Seibert, M Marvin -- Andreasson, Jakob -- Rocker, Andrea -- Jonsson, Olof -- Svenda, Martin -- Stern, Stephan -- Nass, Karol -- Andritschke, Robert -- Schroter, Claus-Dieter -- Krasniqi, Faton -- Bott, Mario -- Schmidt, Kevin E -- Wang, Xiaoyu -- Grotjohann, Ingo -- Holton, James M -- Barends, Thomas R M -- Neutze, Richard -- Marchesini, Stefano -- Fromme, Raimund -- Schorb, Sebastian -- Rupp, Daniela -- Adolph, Marcus -- Gorkhover, Tais -- Andersson, Inger -- Hirsemann, Helmut -- Potdevin, Guillaume -- Graafsma, Heinz -- Nilsson, Bjorn -- Spence, John C H -- 1R01GM095583-01/GM/NIGMS NIH HHS/ -- 1U54GM094625-01/GM/NIGMS NIH HHS/ -- R01 GM095583/GM/NIGMS NIH HHS/ -- U54 GM094599/GM/NIGMS NIH HHS/ -- U54 GM094625/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Feb 3;470(7332):73-7. doi: 10.1038/nature09750.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany. henry.chapman@desy.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21293373" target="_blank"〉PubMed〈/a〉

Description: The morphology of micrometre-size particulate matter is of critical importance in fields ranging from toxicology to climate science, yet these properties are surprisingly difficult to measure in the particles' native environment. Electron microscopy requires collection of particles on a substrate; visible light scattering provides insufficient resolution; and X-ray synchrotron studies have been limited to ensembles of particles. Here we demonstrate an in situ method for imaging individual sub-micrometre particles to nanometre resolution in their native environment, using intense, coherent X-ray pulses from the Linac Coherent Light Source free-electron laser. We introduced individual aerosol particles into the pulsed X-ray beam, which is sufficiently intense that diffraction from individual particles can be measured for morphological analysis. At the same time, ion fragments ejected from the beam were analysed using mass spectrometry, to determine the composition of single aerosol particles. Our results show the extent of internal dilation symmetry of individual soot particles subject to non-equilibrium aggregation, and the surprisingly large variability in their fractal dimensions. More broadly, our methods can be extended to resolve both static and dynamic morphology of general ensembles of disordered particles. Such general morphology has implications in topics such as solvent accessibilities in proteins, vibrational energy transfer by the hydrodynamic interaction of amino acids, and large-scale production of nanoscale structures by flame synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loh, N D -- Hampton, C Y -- Martin, A V -- Starodub, D -- Sierra, R G -- Barty, A -- Aquila, A -- Schulz, J -- Lomb, L -- Steinbrener, J -- Shoeman, R L -- Kassemeyer, S -- Bostedt, C -- Bozek, J -- Epp, S W -- Erk, B -- Hartmann, R -- Rolles, D -- Rudenko, A -- Rudek, B -- Foucar, L -- Kimmel, N -- Weidenspointner, G -- Hauser, G -- Holl, P -- Pedersoli, E -- Liang, M -- Hunter, M S -- Gumprecht, L -- Coppola, N -- Wunderer, C -- Graafsma, H -- Maia, F R N C -- Ekeberg, T -- Hantke, M -- Fleckenstein, H -- Hirsemann, H -- Nass, K -- White, T A -- Tobias, H J -- Farquar, G R -- Benner, W H -- Hau-Riege, S P -- Reich, C -- Hartmann, A -- Soltau, H -- Marchesini, S -- Bajt, S -- Barthelmess, M -- Bucksbaum, P -- Hodgson, K O -- Struder, L -- Ullrich, J -- Frank, M -- Schlichting, I -- Chapman, H N -- Bogan, M J -- England -- Nature. 2012 Jun 27;486(7404):513-7. doi: 10.1038/nature11222.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉PULSE Institute, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22739316" target="_blank"〉PubMed〈/a〉

Description: Photosynthesis, a process catalysed by plants, algae and cyanobacteria converts sunlight to energy thus sustaining all higher life on Earth. Two large membrane protein complexes, photosystem I and II (PSI and PSII), act in series to catalyse the light-driven reactions in photosynthesis. PSII catalyses the light-driven water splitting process, which maintains the Earth's oxygenic atmosphere. In this process, the oxygen-evolving complex (OEC) of PSII cycles through five states, S0 to S4, in which four electrons are sequentially extracted from the OEC in four light-driven charge-separation events. Here we describe time resolved experiments on PSII nano/microcrystals from Thermosynechococcus elongatus performed with the recently developed technique of serial femtosecond crystallography. Structures have been determined from PSII in the dark S1 state and after double laser excitation (putative S3 state) at 5 and 5.5 A resolution, respectively. The results provide evidence that PSII undergoes significant conformational changes at the electron acceptor side and at the Mn4CaO5 core of the OEC. These include an elongation of the metal cluster, accompanied by changes in the protein environment, which could allow for binding of the second substrate water molecule between the more distant protruding Mn (referred to as the 'dangler' Mn) and the Mn3CaOx cubane in the S2 to S3 transition, as predicted by spectroscopic and computational studies. This work shows the great potential for time-resolved serial femtosecond crystallography for investigation of catalytic processes in biomolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kupitz, Christopher -- Basu, Shibom -- Grotjohann, Ingo -- Fromme, Raimund -- Zatsepin, Nadia A -- Rendek, Kimberly N -- Hunter, Mark S -- Shoeman, Robert L -- White, Thomas A -- Wang, Dingjie -- James, Daniel -- Yang, Jay-How -- Cobb, Danielle E -- Reeder, Brenda -- Sierra, Raymond G -- Liu, Haiguang -- Barty, Anton -- Aquila, Andrew L -- Deponte, Daniel -- Kirian, Richard A -- Bari, Sadia -- Bergkamp, Jesse J -- Beyerlein, Kenneth R -- Bogan, Michael J -- Caleman, Carl -- Chao, Tzu-Chiao -- Conrad, Chelsie E -- Davis, Katherine M -- Fleckenstein, Holger -- Galli, Lorenzo -- Hau-Riege, Stefan P -- Kassemeyer, Stephan -- Laksmono, Hartawan -- Liang, Mengning -- Lomb, Lukas -- Marchesini, Stefano -- Martin, Andrew V -- Messerschmidt, Marc -- Milathianaki, Despina -- Nass, Karol -- Ros, Alexandra -- Roy-Chowdhury, Shatabdi -- Schmidt, Kevin -- Seibert, Marvin -- Steinbrener, Jan -- Stellato, Francesco -- Yan, Lifen -- Yoon, Chunhong -- Moore, Thomas A -- Moore, Ana L -- Pushkar, Yulia -- Williams, Garth J -- Boutet, Sebastien -- Doak, R Bruce -- Weierstall, Uwe -- Frank, Matthias -- Chapman, Henry N -- Spence, John C H -- Fromme, Petra -- 1R01GM095583/GM/NIGMS NIH HHS/ -- R01 GM095583/GM/NIGMS NIH HHS/ -- England -- Nature. 2014 Sep 11;513(7517):261-5. doi: 10.1038/nature13453. Epub 2014 Jul 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA [2]. ; Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA. ; Department of Physics, Arizona State University, Tempe, Arizona 85287, USA. ; 1] Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA [2] Lawrence Livermore National Laboratory, Livermore, California 94550, USA. ; Max-Planck-Institut fur medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany. ; Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany. ; Stanford PULSE Institute, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] European XFEL GmbH, Notkestrasse 85, 22607 Hamburg, Germany. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] Linac Coherent Light Source, Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA. ; 1] Department of Physics, Arizona State University, Tempe, Arizona 85287, USA [2] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany. ; 1] Max Planck Advanced Study Group, Center for Free-Electron Laser Science (CFEL), Notkestrasse 85, 22607 Hamburg, Germany [2] Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, 69117 Heidelberg, Germany. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] Department of Physics and Astronomy, Uppsala University, Regementsvagen 1, SE-752 37 Uppsala, Sweden. ; 1] Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287-1604, USA [2] University of Regina, 3737 Wascana Pkwy Regina, Saskatchewan S4S 0A2, Canada. ; Department of Physics, Purdue University, 525 Northwestern Avenue, West Lafayette, Indiana 47907, USA. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany. ; Lawrence Livermore National Laboratory, Livermore, California 94550, USA. ; 1] Max-Planck-Institut fur medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany [2] Max Planck Advanced Study Group, Center for Free-Electron Laser Science (CFEL), Notkestrasse 85, 22607 Hamburg, Germany. ; Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] Department ARC Centre of Excellence for Coherent X-ray Science, Department of Physics, University of Melbourne, Parkville VIC 3010, Australia. ; Linac Coherent Light Source, Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA. ; 1] Max-Planck-Institut fur medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany [2] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [3] University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany. ; 1] Linac Coherent Light Source, Stanford Linear Accelerator Center (SLAC) National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA [2] Uppsala University, Sankt Olofsgatan 10B, 753 12 Uppsala, Sweden. ; 1] Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany [2] University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany [3] Center for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25043005" target="_blank"〉PubMed〈/a〉

Description: The determination of protein crystal structures is hampered by the need for macroscopic crystals. X-ray free-electron lasers (FELs) provide extremely intense pulses of femtosecond duration, which allow data collection from nanometre- to micrometre-sized crystals in a 'diffraction-before-destruction' approach. So far, all protein structure determinations carried out using FELs have been based on previous knowledge of related, known structures. Here we show that X-ray FEL data can be used for de novo protein structure determination, that is, without previous knowledge about the structure. Using the emerging technique of serial femtosecond crystallography, we performed single-wavelength anomalous scattering measurements on microcrystals of the well-established model system lysozyme, in complex with a lanthanide compound. Using Monte-Carlo integration, we obtained high-quality diffraction intensities from which experimental phases could be determined, resulting in an experimental electron density map good enough for automated building of the protein structure. This demonstrates the feasibility of determining novel protein structures using FELs. We anticipate that serial femtosecond crystallography will become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barends, Thomas R M -- Foucar, Lutz -- Botha, Sabine -- Doak, R Bruce -- Shoeman, Robert L -- Nass, Karol -- Koglin, Jason E -- Williams, Garth J -- Boutet, Sebastien -- Messerschmidt, Marc -- Schlichting, Ilme -- England -- Nature. 2014 Jan 9;505(7482):244-7. doi: 10.1038/nature12773. Epub 2013 Nov 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany. ; 1] Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany [2] Department of Physics, Arizona State University, PO Box 871504, Tempe, Arizona 85287-1504, USA. ; SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24270807" target="_blank"〉PubMed〈/a〉

Description: Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788707/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788707/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boutet, Sebastien -- Lomb, Lukas -- Williams, Garth J -- Barends, Thomas R M -- Aquila, Andrew -- Doak, R Bruce -- Weierstall, Uwe -- DePonte, Daniel P -- Steinbrener, Jan -- Shoeman, Robert L -- Messerschmidt, Marc -- Barty, Anton -- White, Thomas A -- Kassemeyer, Stephan -- Kirian, Richard A -- Seibert, M Marvin -- Montanez, Paul A -- Kenney, Chris -- Herbst, Ryan -- Hart, Philip -- Pines, Jack -- Haller, Gunther -- Gruner, Sol M -- Philipp, Hugh T -- Tate, Mark W -- Hromalik, Marianne -- Koerner, Lucas J -- van Bakel, Niels -- Morse, John -- Ghonsalves, Wilfred -- Arnlund, David -- Bogan, Michael J -- Caleman, Carl -- Fromme, Raimund -- Hampton, Christina Y -- Hunter, Mark S -- Johansson, Linda C -- Katona, Gergely -- Kupitz, Christopher -- Liang, Mengning -- Martin, Andrew V -- Nass, Karol -- Redecke, Lars -- Stellato, Francesco -- Timneanu, Nicusor -- Wang, Dingjie -- Zatsepin, Nadia A -- Schafer, Donald -- Defever, James -- Neutze, Richard -- Fromme, Petra -- Spence, John C H -- Chapman, Henry N -- Schlichting, Ilme -- 1R01GM095583/GM/NIGMS NIH HHS/ -- R01 GM095583/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 20;337(6092):362-4. doi: 10.1126/science.1217737. Epub 2012 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA. sboutet@slac.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22653729" target="_blank"〉PubMed〈/a〉

Description: The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, is a promising target to develop new treatments against sleeping sickness, a fatal disease caused by this protozoan parasite. The structure of the mature, active form of TbCatB has so far not provided sufficient information for the design of a safe and specific drug against T. brucei. By combining two recent innovations, in vivo crystallization and serial femtosecond crystallography, we obtained the room-temperature 2.1 angstrom resolution structure of the fully glycosylated precursor complex of TbCatB. The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the "diffraction-before-destruction" approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3786669/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3786669/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redecke, Lars -- Nass, Karol -- DePonte, Daniel P -- White, Thomas A -- Rehders, Dirk -- Barty, Anton -- Stellato, Francesco -- Liang, Mengning -- Barends, Thomas R M -- Boutet, Sebastien -- Williams, Garth J -- Messerschmidt, Marc -- Seibert, M Marvin -- Aquila, Andrew -- Arnlund, David -- Bajt, Sasa -- Barth, Torsten -- Bogan, Michael J -- Caleman, Carl -- Chao, Tzu-Chiao -- Doak, R Bruce -- Fleckenstein, Holger -- Frank, Matthias -- Fromme, Raimund -- Galli, Lorenzo -- Grotjohann, Ingo -- Hunter, Mark S -- Johansson, Linda C -- Kassemeyer, Stephan -- Katona, Gergely -- Kirian, Richard A -- Koopmann, Rudolf -- Kupitz, Chris -- Lomb, Lukas -- Martin, Andrew V -- Mogk, Stefan -- Neutze, Richard -- Shoeman, Robert L -- Steinbrener, Jan -- Timneanu, Nicusor -- Wang, Dingjie -- Weierstall, Uwe -- Zatsepin, Nadia A -- Spence, John C H -- Fromme, Petra -- Schlichting, Ilme -- Duszenko, Michael -- Betzel, Christian -- Chapman, Henry N -- 1R01GM095583/GM/NIGMS NIH HHS/ -- R01 GM095583/GM/NIGMS NIH HHS/ -- U54 GM094599/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Jan 11;339(6116):227-30. doi: 10.1126/science.1229663. Epub 2012 Nov 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joint Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, and Institute of Biochemistry, University of Lubeck, at Deutsches Elektronen-Synchrotron, Notkestrasse 85, 22607 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23196907" target="_blank"〉PubMed〈/a〉

Description: The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barends, Thomas R M -- Foucar, Lutz -- Ardevol, Albert -- Nass, Karol -- Aquila, Andrew -- Botha, Sabine -- Doak, R Bruce -- Falahati, Konstantin -- Hartmann, Elisabeth -- Hilpert, Mario -- Heinz, Marcel -- Hoffmann, Matthias C -- Kofinger, Jurgen -- Koglin, Jason E -- Kovacsova, Gabriela -- Liang, Mengning -- Milathianaki, Despina -- Lemke, Henrik T -- Reinstein, Jochen -- Roome, Christopher M -- Shoeman, Robert L -- Williams, Garth J -- Burghardt, Irene -- Hummer, Gerhard -- Boutet, Sebastien -- Schlichting, Ilme -- New York, N.Y. -- Science. 2015 Oct 23;350(6259):445-50. doi: 10.1126/science.aac5492. Epub 2015 Sep 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany. thomas.barends@mpimf-heidelberg.mpg.de ilme.schlichting@mpimf-heidelberg.mpg.de. ; Max-Planck-Institut fur Medizinische Forschung, Jahnstrasse 29, 69120 Heidelberg, Germany. ; Max-Planck-Institut fur Biophysik, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany. ; European XFEL GmbH, Albert-Einstein-Ring 19, 22761 Hamburg, Germany. ; Institut fur Physikalische und Theoretische Chemie, Goethe-Universitat, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main, Germany. ; Max-Planck-Institut fur Biophysik, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany. Institut fur Physikalische und Theoretische Chemie, Goethe-Universitat, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main, Germany. ; Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26359336" target="_blank"〉PubMed〈/a〉