6S0Q

Structure of the A2A adenosine receptor determined at SwissFEL using native-SAD at 4.57 keV from 50,000 diffraction patterns

Summary for 6S0Q

• Entry DOI: 10.2210/pdb6s0q/pdb
• Related: 6S0L
• Descriptor: Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a, 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol, OLEIC ACID, ... (6 entities in total)
• Functional Keywords: native-sad, serial femtosecond crystallography, sfx, swissfel, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 52897.43

Authors

Nass, K.,Cheng, R.,Vera, L.,Mozzanica, A.,Redford, S.,Ozerov, D.,Basu, S.,James, D.,Knopp, G.,Cirelli, C.,Martiel, I.,Casadei, C.,Weinert, T.,Nogly, P.,Skopintsev, P.,Usov, I.,Leonarski, F.,Geng, T.,Rappas, M.,Dore, A.S.,Cooke, R.,Nasrollahi Shirazi, S.,Dworkowski, F.,Sharpe, M.,Olieric, N.,Steinmetz, M.O.,Schertler, G.,Abela, R.,Patthey, L.,Schmitt, B.,Hennig, M.,Standfuss, J.,Wang, M.,Milne, J.C. (deposition date: 2019-06-18, release date: 2020-07-15, Last modification date: 2024-11-13)

Primary citation

Nass, K.,Cheng, R.,Vera, L.,Mozzanica, A.,Redford, S.,Ozerov, D.,Basu, S.,James, D.,Knopp, G.,Cirelli, C.,Martiel, I.,Casadei, C.,Weinert, T.,Nogly, P.,Skopintsev, P.,Usov, I.,Leonarski, F.,Geng, T.,Rappas, M.,Dore, A.S.,Cooke, R.,Nasrollahi Shirazi, S.,Dworkowski, F.,Sharpe, M.,Olieric, N.,Bacellar, C.,Bohinc, R.,Steinmetz, M.O.,Schertler, G.,Abela, R.,Patthey, L.,Schmitt, B.,Hennig, M.,Standfuss, J.,Wang, M.,Milne, C.J.
Advances in long-wavelength native phasing at X-ray free-electron lasers.
Iucrj, 7:965-975, 2020

PubMed Abstract: Long-wavelength pulses from the Swiss X-ray free-electron laser (XFEL) have been used for protein structure determination by native single-wavelength anomalous diffraction (native-SAD) phasing of serial femtosecond crystallography (SFX) data. In this work, sensitive anomalous data-quality indicators and model proteins were used to quantify improvements in native-SAD at XFELs such as utilization of longer wavelengths, careful experimental geometry optimization, and better post-refinement and partiality correction. Compared with studies using shorter wavelengths at other XFELs and older software versions, up to one order of magnitude reduction in the required number of indexed images for native-SAD was achieved, hence lowering sample consumption and beam-time requirements significantly. Improved data quality and higher anomalous signal facilitate so-far underutilized structure determination of challenging proteins at XFELs. Improvements presented in this work can be used in other types of SFX experiments that require accurate measurements of weak signals, for example time-resolved studies.

PubMed: 33209311
DOI: 10.1107/S2052252520011379

Experimental method

X-RAY DIFFRACTION (2.65 Å)