5O4C
From macrocrystals to microcrystals: a strategy for membrane protein serial crystallography
Summary for 5O4C
| Entry DOI | 10.2210/pdb5o4c/pdb |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, BACTERIOCHLOROPHYLL B, BACTERIOPHEOPHYTIN B, ... (15 entities in total) |
| Functional Keywords | membrane photosynthetic wild-type xfel, membrane protein |
| Biological source | Blastochloris viridis More |
| Total number of polymer chains | 4 |
| Total formula weight | 144533.44 |
| Authors | Dods, R.,Baath, P.,Branden, G.,Neutze, R. (deposition date: 2017-05-28, release date: 2017-08-16, Last modification date: 2024-01-17) |
| Primary citation | Dods, R.,Bath, P.,Arnlund, D.,Beyerlein, K.R.,Nelson, G.,Liang, M.,Harimoorthy, R.,Berntsen, P.,Malmerberg, E.,Johansson, L.,Andersson, R.,Bosman, R.,Carbajo, S.,Claesson, E.,Conrad, C.E.,Dahl, P.,Hammarin, G.,Hunter, M.S.,Li, C.,Lisova, S.,Milathianaki, D.,Robinson, J.,Safari, C.,Sharma, A.,Williams, G.,Wickstrand, C.,Yefanov, O.,Davidsson, J.,DePonte, D.P.,Barty, A.,Branden, G.,Neutze, R. From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography. Structure, 25:1461-1468.e2, 2017 Cited by PubMed Abstract: Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RC). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RC serial femtosecond crystallography (SFX) structure from 3.3-Å to 2.4-Å resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography. PubMed: 28781082DOI: 10.1016/j.str.2017.07.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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