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  1. Article ; Online: Crystallization of a self-assembled three-dimensional DNA nanostructure.

    Rendek, Kimberly N / Fromme, Raimund / Grotjohann, Ingo / Fromme, Petra

    Acta crystallographica. Section F, Structural biology and crystallization communications

    2013  Volume 69, Issue Pt 2, Page(s) 141–146

    Abstract: The powerful and specific molecular-recognition system present in the base-pairing of DNA allows for the design of a plethora of nanostructures. In this work, the crystallization of a self-assembling three-dimensional B-DNA nanostructure is described. ... ...

    Abstract The powerful and specific molecular-recognition system present in the base-pairing of DNA allows for the design of a plethora of nanostructures. In this work, the crystallization of a self-assembling three-dimensional B-DNA nanostructure is described. The DNA nanostructure consists of six single-stranded oligonucleotides that hybridize to form a three-dimensional tetrahedron of 80 kDa in molecular mass and 20 bp on each edge. Crystals of the tetrahedron have been successfully produced and characterized. These crystals may form the basis for an X-ray structure of the tetrahedron in the future. Nucleotide crystallography poses many challenges, leading to the fact that only 1352 X-ray structures of nucleic acids have been solved compared with more than 80,000 protein structures. In this work, the crystallization optimization for three-dimensional tetrahedra is also described, with the eventual goal of producing nanocrystals to overcome the radiation-damage obstacle by the use of free-electron laser technology in the future.
    MeSH term(s) Crystallization ; Crystallography, X-Ray ; DNA/chemistry ; Nanostructures/chemistry ; Nucleic Acid Conformation
    Chemical Substances DNA (9007-49-2)
    Language English
    Publishing date 2013-01-31
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1744-3091
    ISSN (online) 1744-3091
    DOI 10.1107/S1744309112052128
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser.

    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, Sébastien / Doak, R Bruce / Weierstall, Uwe / Frank, Matthias / Chapman, Henry N / Spence, John C H / Fromme, Petra

    Nature

    2014  Volume 513, Issue 7517, Page(s) 261–265

    Abstract: 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- ... ...

    Abstract 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 Å 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.
    MeSH term(s) Crystallography, X-Ray ; Cyanobacteria/chemistry ; Models, Molecular ; Photosystem II Protein Complex/chemistry ; Protein Structure, Tertiary
    Chemical Substances Photosystem II Protein Complex
    Language English
    Publishing date 2014-07-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature13453
    Database MEDical Literature Analysis and Retrieval System OnLINE

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