4ETA

Lysozyme, room temperature, 400 kGy dose

4ETA の概要

• エントリーDOI: 10.2210/pdb4eta/pdb
• 関連するPDBエントリー: 4ET8 4ET9 4ETB 4ETC 4ETD 4ETE
• 分子名称: Lysozyme C, CHLORIDE ION (3 entities in total)
• 機能のキーワード: lysozyme, hydrolase
• 由来する生物種: Gallus gallus (bantam,chickens)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14366.61

構造登録者

Boutet, S.,Lomb, L.,Williams, G.,Barends, T.,Aquila, A.,Doak, R.B.,Weierstall, U.,DePonte, D.,Steinbrener, J.,Shoeman, R.,Messerschmidt, M.,Barty, A.,White, T.,Kassemeyer, S.,Kirian, R.,Seibert, M.,Montanez, P.,Kenney, C.,Herbst, R.,Hart, P.,Pines, J.,Haller, G.,Gruner, S.,Philllip, H.,Tate, M.,Hromalik, M.,Koerner, L.,van Bakel, N.,Morse, J.,Ghonsalves, W.,Arnlund, D.,Bogan, M.,Calemann, C.,Fromme, R.,Hampton, C.,Hunter, M.,Johansson, L.,Katona, G.,Kupitz, C.,Liang, M.,Martin, A.,Nass, K.,Redecke, L.,Stellato, F.,Timneanu, N.,Wang, D.,Zatsepin, N.,Schafer, D.,Defever, K.,Neutze, R.,Fromme, P.,Spence, J.,Chapman, H.,Schlichting, I. (登録日: 2012-04-24, 公開日: 2012-06-13, 最終更新日: 2017-11-15)

主引用文献

Boutet, S.,Lomb, L.,Williams, G.J.,Barends, T.R.,Aquila, A.,Doak, R.B.,Weierstall, U.,DePonte, D.P.,Steinbrener, J.,Shoeman, R.L.,Messerschmidt, M.,Barty, A.,White, T.A.,Kassemeyer, S.,Kirian, R.A.,Seibert, M.M.,Montanez, P.A.,Kenney, C.,Herbst, R.,Hart, P.,Pines, J.,Haller, G.,Gruner, S.M.,Philipp, H.T.,Tate, M.W.,Hromalik, M.,Koerner, L.J.,van Bakel, N.,Morse, J.,Ghonsalves, W.,Arnlund, D.,Bogan, M.J.,Caleman, C.,Fromme, R.,Hampton, C.Y.,Hunter, M.S.,Johansson, L.C.,Katona, G.,Kupitz, C.,Liang, M.,Martin, A.V.,Nass, K.,Redecke, L.,Stellato, F.,Timneanu, N.,Wang, D.,Zatsepin, N.A.,Schafer, D.,Defever, J.,Neutze, R.,Fromme, P.,Spence, J.C.,Chapman, H.N.,Schlichting, I.
High-resolution protein structure determination by serial femtosecond crystallography.
Science, 337:362-364, 2012

PubMed Abstract: Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

PubMed: 22653729
DOI: 10.1126/science.1217737

実験手法

X-RAY DIFFRACTION (1.91 Å)