6gwa
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CONB_CANEN CONB_CANEN]] May act as a carbohydrate-binding protein. | [[http://www.uniprot.org/uniprot/CONB_CANEN CONB_CANEN]] May act as a carbohydrate-binding protein. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10-120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 mum XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined. | ||
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+ | Megahertz data collection from protein microcrystals at an X-ray free-electron laser.,Grunbein ML, Bielecki J, Gorel A, Stricker M, Bean R, Cammarata M, Dorner K, Frohlich L, Hartmann E, Hauf S, Hilpert M, Kim Y, Kloos M, Letrun R, Messerschmidt M, Mills G, Nass Kovacs G, Ramilli M, Roome CM, Sato T, Scholz M, Sliwa M, Sztuk-Dambietz J, Weik M, Weinhausen B, Al-Qudami N, Boukhelef D, Brockhauser S, Ehsan W, Emons M, Esenov S, Fangohr H, Kaukher A, Kluyver T, Lederer M, Maia L, Manetti M, Michelat T, Munnich A, Pallas F, Palmer G, Previtali G, Raab N, Silenzi A, Szuba J, Venkatesan S, Wrona K, Zhu J, Doak RB, Shoeman RL, Foucar L, Colletier JP, Mancuso AP, Barends TRM, Stan CA, Schlichting I Nat Commun. 2018 Aug 28;9(1):3487. doi: 10.1038/s41467-018-05953-4. PMID:30154468<ref>PMID:30154468</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6gwa" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 07:55, 12 September 2018
Concanavalin B structure determined with data from the EuXFEL, the first MHz free electron laser
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Categories: Canavalia ensiformis | Barends, T R.M | Bean, R | Bielecki, J | Colletier, J P | Doak, R B | Doerner, K | Foucar, L | Gorel, A | Gruenbein, M L | Hartmann, E | Hilpert, M | Kloos, M | Letrun, R | Mancuso, A | Meserschmidt, M | Nass-Kovacs, G | Ramilli, M | Roome, C M | Sato, T | Schlichting, I | Shoeman, R L | Stan, C | Stricker, M | Sztuk-Dambietz, J | Free-electron laser | Lectin | Serial crystallography | Sugar binding protein