Concanavalin A structure determined with data from the EuXFEL, the first MHz free electron laser
Structural highlights
6gw9 is a 1 chain structure with sequence from Canavalia cathartica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[CONV_CANCT] D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order (PubMed:24519628, PubMed:27737777). Also binds to serum fetuin and ovalbumin (PubMed:24519628). Has hemagglutinating activity towards rabbit erythrocytes (PubMed:24519628). Is not toxic towards larvae of the brine shrimp Artemia (PubMed:24519628). Induces relaxation in rat endothelized aorta (PubMed:24519628). Shows a transient edematogenic effect in rat (PubMed:27737777).[1][2]
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Osterne VJ, Santiago MQ, Pinto-Junior VR, Cajazeiras JB, Correia JL, Leitao CC, Carneiro RF, Pereira-Junior FN, Vasconcelos MA, Rocha BA, Assreuy AM, Bringel PH, Nagano CS, Nascimento KS, Cavada BS. Purification, partial characterization, and CNBr-sepharose immobilization of a vasorelaxant glucose/mannose lectin from Canavalia virosa seeds. Appl Biochem Biotechnol. 2014 Apr;172(7):3342-53. doi: 10.1007/s12010-014-0751-3., Epub 2014 Feb 13. PMID:24519628 doi:http://dx.doi.org/10.1007/s12010-014-0751-3
↑ Osterne VJ, Silva-Filho JC, Santiago MQ, Pinto-Junior VR, Almeida AC, Barreto AA, Wolin IA, Nascimento AP, Amorim RM, Rocha BA, Delatorre P, Nagano CS, Leal RB, Assreuy AM, Nascimento KS, Cavada BS. Structural characterization of a lectin from Canavalia virosa seeds with inflammatory and cytotoxic activities. Int J Biol Macromol. 2016 Oct 11;94(Pt A):271-282. doi:, 10.1016/j.ijbiomac.2016.10.020. PMID:27737777 doi:http://dx.doi.org/10.1016/j.ijbiomac.2016.10.020
↑ 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. Megahertz data collection from protein microcrystals at an X-ray free-electron laser. Nat Commun. 2018 Aug 28;9(1):3487. doi: 10.1038/s41467-018-05953-4. PMID:30154468 doi:http://dx.doi.org/10.1038/s41467-018-05953-4
