3PCQ

Femtosecond X-ray protein Nanocrystallography

3PCQ の概要

• エントリーDOI: 10.2210/pdb3pcq/pdb
• 関連するPDBエントリー: 1JB0
• 分子名称: Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit XI, Photosystem I reaction center subunit XII, ... (20 entities in total)
• 機能のキーワード: membrane protein, multiprotein-pigment complex, photosynthesis
• 由来する生物種: Thermosynechococcus elongatus; 詳細
• 細胞内の位置: Cellular thylakoid membrane ; Multi- pass membrane protein : P0A405 Q8DGB4 P0A407 P0A425; Cellular thylakoid membrane ; Single-pass membrane protein : P0A403 P0A427 P0A429; Cellular thylakoid membrane ; Peripheral membrane protein ; Cytoplasmic side : P0A415; Cellular thylakoid membrane ; Peripheral membrane protein : P0A423
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 359828.36

構造登録者

Chapman, H.N.,Fromme, P.,Barty, A.,White, T.A.,Kirian, R.A.,Aquila, A.,Hunter, M.S.,Schulz, J.,Deponte, D.P.,Weierstall, U.,Doak, R.B.,Maia, F.R.N.C.,Martin, A.V.,Schlichting, I.,Lomb, L.,Coppola, N.,Shoeman, R.L.,Epp, S.W.,Hartmann, R.,Rolles, D.,Rudenko, A.,Foucar, L.,Kimmel, N.,Weidenspointner, G.,Holl, P.,Liang, M.,Barthelmess, M.,Caleman, C.,Boutet, S.,Bogan, M.J.,Krzywinski, J.,Bostedt, C.,Bajt, S.,Gumprecht, L.,Rudek, B.,Erk, B.,Schmidt, C.,Homke, A.,Reich, C.,Pietschner, D.,Struder, L.,Hauser, G.,Gorke, H.,Ullrich, J.,Herrmann, S.,Schaller, G.,Schopper, F.,Soltau, H.,Kuhnel, K.-U.,Messerschmidt, M.,Bozek, J.D.,Hau-Riege, S.P.,Frank, M.,Hampton, C.Y.,Sierra, R.,Starodub, D.,Williams, G.J.,Hajdu, J.,Timneanu, N.,Seibert, M.M.,Andreasson, J.,Rocker, A.,Jonsson, O.,Svenda, M.,Stern, S.,Nass, K.,Andritschke, R.,Schroter, C.-D.,Krasniqi, F.,Bott, M.,Schmidt, K.E.,Wang, X.,Grotjohann, I.,Holton, J.M.,Barends, T.R.M.,Neutze, R.,Marchesini, S.,Fromme, R.,Schorb, S.,Rupp, D.,Adolph, M.,Gorkhover, T.,Andersson, I.,Hirsemann, H.,Potdevin, G.,Graafsma, H.,Nilsson, B.,Spence, J.C.H. (登録日: 2010-10-21, 公開日: 2011-02-02, 最終更新日: 2024-10-30)

主引用文献

Chapman, H.N.,Fromme, P.,Barty, A.,White, T.A.,Kirian, R.A.,Aquila, A.,Hunter, M.S.,Schulz, J.,Deponte, D.P.,Weierstall, U.,Doak, R.B.,Maia, F.R.,Martin, A.V.,Schlichting, I.,Lomb, L.,Coppola, N.,Shoeman, R.L.,Epp, S.W.,Hartmann, R.,Rolles, D.,Rudenko, A.,Foucar, L.,Kimmel, N.,Weidenspointner, G.,Holl, P.,Liang, M.,Barthelmess, M.,Caleman, C.,Boutet, S.,Bogan, M.J.,Krzywinski, J.,Bostedt, C.,Bajt, S.,Gumprecht, L.,Rudek, B.,Erk, B.,Schmidt, C.,Homke, A.,Reich, C.,Pietschner, D.,Struder, L.,Hauser, G.,Gorke, H.,Ullrich, J.,Herrmann, S.,Schaller, G.,Schopper, F.,Soltau, H.,Kuhnel, K.U.,Messerschmidt, M.,Bozek, J.D.,Hau-Riege, S.P.,Frank, M.,Hampton, C.Y.,Sierra, R.G.,Starodub, D.,Williams, G.J.,Hajdu, J.,Timneanu, N.,Seibert, M.M.,Andreasson, J.,Rocker, A.,Jonsson, O.,Svenda, M.,Stern, S.,Nass, K.,Andritschke, R.,Schroter, C.D.,Krasniqi, F.,Bott, M.,Schmidt, K.E.,Wang, X.,Grotjohann, I.,Holton, J.M.,Barends, T.R.,Neutze, R.,Marchesini, S.,Fromme, R.,Schorb, S.,Rupp, D.,Adolph, M.,Gorkhover, T.,Andersson, I.,Hirsemann, H.,Potdevin, G.,Graafsma, H.,Nilsson, B.,Spence, J.C.
Femtosecond X-ray protein nanocrystallography.
Nature, 470:73-77, 2011

PubMed Abstract: X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction 'snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (∼200 nm to 2 μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.

PubMed: 21293373
DOI: 10.1038/nature09750

実験手法

X-RAY DIFFRACTION (8.984 Å)