6H0K
Hen egg-white lysozyme structure determined with data from the EuXFEL, the first MHz free electron laser, 7.47 keV photon energy
6H0K の概要
| エントリーDOI | 10.2210/pdb6h0k/pdb |
| 分子名称 | Lysozyme C (2 entities in total) |
| 機能のキーワード | free-electron laser, serial crystallography, lectin, hydrolase |
| 由来する生物種 | Gallus gallus (Chicken) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14331.16 |
| 構造登録者 | Gruenbein, M.L.,Gorel, A.,Stricker, M.,Bean, R.,Bielecki, J.,Doerner, K.,Hartmann, E.,Hilpert, M.,Kloos, M.,Letrun, R.,Sztuk-Dambietz, J.,Mancuso, A.,Meserschmidt, M.,Nass-Kovacs, G.,Ramilli, M.,Roome, C.M.,Sato, T.,Doak, R.B.,Shoeman, R.L.,Foucar, L.,Colletier, J.P.,Barends, T.R.M.,Stan, C.,Schlichting, I. (登録日: 2018-07-10, 公開日: 2018-09-05, 最終更新日: 2024-10-23) |
| 主引用文献 | Grunbein, M.L.,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, C.M.,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, R.B.,Shoeman, R.L.,Foucar, L.,Colletier, J.P.,Mancuso, A.P.,Barends, T.R.M.,Stan, C.A.,Schlichting, I. Megahertz data collection from protein microcrystals at an X-ray free-electron laser. Nat Commun, 9:3487-3487, 2018 Cited by PubMed Abstract: 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 μm 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. PubMed: 30154468DOI: 10.1038/s41467-018-05953-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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