Zobrazeno 1 - 10
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pro vyhledávání: '"in crystallo optical spectroscopy"'
Akademický článek
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Autor:
Demet Kekilli, Tadeo Moreno-Chicano, Amanda K. Chaplin, Sam Horrell, Florian S. N. Dworkowski, Jonathan A. R. Worrall, Richard W. Strange, Michael A. Hough
Publikováno v:
IUCrJ, Vol 4, Iss 3, Pp 263-270 (2017)
Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into r
Externí odkaz:
https://doaj.org/article/8b2bf4548c0b4d05886fcd59e4cd3373
Akademický článek
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Autor:
Richard W. Strange, Sam Horrell, Demet Kekilli, Amanda K. Chaplin, Florian S. N. Dworkowski, T. Moreno-Chicano, Jonathan A. R. Worrall, Michael A. Hough
Publikováno v:
'IUCrJ ', vol: 4, pages: 263-270 (2017)
IUCrJ, Vol 4, Iss 3, Pp 263-270 (2017)
IUCrJ
IUCrJ, Vol 4, Iss 3, Pp 263-270 (2017)
IUCrJ
Integrated structural biology can yield powerful synergies and maximize the biological information gained. Two examples are described of combining X-ray crystallography with single-crystal resonance Raman and UV–visible spectroscopies to study the
Autor:
Dominique Bourgeois
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2017, 18 (6), pp.E1187. ⟨10.3390/ijms18061187⟩
International Journal of Molecular Sciences, 2017, 18 (6), pp.E1187. ⟨10.3390/ijms18061187⟩
International Journal of Molecular Sciences, MDPI, 2017, 18 (6), pp.E1187. ⟨10.3390/ijms18061187⟩
International Journal of Molecular Sciences, 2017, 18 (6), pp.E1187. ⟨10.3390/ijms18061187⟩
International audience; Because they enable labeling of biological samples in a genetically-encoded manner, Fluorescent Proteins (FPs) have revolutionized life sciences. Photo-transformable fluorescent proteins (PTFPs), in particular, recently attrac
Autor:
Eriko Nango, Jörg Standfuss, Shigeki Owada, Takanori Nakane, Petra Båth, Robert Dods, Ayumi Yamashita, Byeonghyun Jeon, Minoru Kubo, Takaaki Fujiwara, Jan Davidsson, Rebecka Andersson, Dohyun Im, Michihiro Sugahara, Yasuaki Yamanaka, Kazumasa Oda, Makina Yabashi, Osamu Nureki, Takaki Hatsui, Kensuke Tono, Tomoyuki Tanaka, Michio Murata, Gebhard F. X. Schertler, Antoine Royant, Daewoong Nam, Takashi Nomura, Eiichi Mizohata, Satoshi Kawatake, Tetsunari Kimura, So Iwata, Przemyslaw Nogly, Tatsuro Shimamura, Takashi Kameshima, Changyong Song, Masahiro Fukuda, Jun Kobayashi, Shigeru Matsuoka, Yasumasa Joti, Ana-Nicoleta Bondar, Richard Neutze, Cecilia Wickstrand, Toshiaki Hosaka, Rie Tanaka, Toshi Arima, Tomohiro Nishizawa
Publikováno v:
Science
Science, American Association for the Advancement of Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Science, American Association for the Advancement of Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Science, 2016, 354 (6319), pp.1552-1557. ⟨10.1126/science.aah3497⟩
Snapshots of bacteriorhodopsin Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallograp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34ff6203187afd15f42f16cdf767fb68
https://hal.univ-grenoble-alpes.fr/hal-01437084
https://hal.univ-grenoble-alpes.fr/hal-01437084
Autor:
Guillaume Gotthard, Antoine Royant, Damien Clavel, David von Stetten, Hélène Pasquier, Daniele de Sanctis, Gerard G. Lambert, Nathan C. Shaner
Publikováno v:
Acta crystallographica. Section D, Structural biology
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2016, 72 (12), pp.1298-1307. ⟨10.1107/S2059798316018623⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2016, 72 (12), pp.1298-1307. ⟨10.1107/S2059798316018623⟩
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2016, 72 (12), pp.1298-1307. ⟨10.1107/S2059798316018623⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2016, 72 (12), pp.1298-1307. ⟨10.1107/S2059798316018623⟩
Until recently, genes coding for homologues of the autofluorescent protein GFP had only been identified in marine organisms from the phyla Cnidaria and Arthropoda. New fluorescent-protein genes have now been found in the phylum Chordata, coding for p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b30e320034c4a692e318625463862edd
https://europepmc.org/articles/PMC5137226/
https://europepmc.org/articles/PMC5137226/
Autor:
David Flot, Fabien Dobias, Thierry Giraud, Gordon A. Leonard, Antoine Royant, Christoph Mueller-Dieckmann, M. Terrien, David von Stetten, Daniele de Sanctis, Franc Sever, Douglas H. Juers, Philippe Carpentier
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2015, 71 (Pt 1), pp.15-26
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (Pt 1), pp.15-26
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2015, 71 (Pt 1), pp.15-26
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (Pt 1), pp.15-26
The current version of the Cryobench in crystallo optical spectroscopy facility of the ESRF is presented. The diverse experiments that can be performed at the Cryobench are also reviewed.
The analysis of structural data obtained by X-ray crystal
The analysis of structural data obtained by X-ray crystal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7f504ce6453628480888a5636e2e4ae
https://hal.univ-grenoble-alpes.fr/hal-01131843
https://hal.univ-grenoble-alpes.fr/hal-01131843
Akademický článek
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Akademický článek
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