5m7l

Blastochloris viridis photosynthetic reaction center synchrotron structure

spinqualitylabelsall models 5m7l, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m7l is a 4 chain structure with sequence from Blastochloris viridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCL, BPB, DGA, FE2, HEC, MPG, MQ7, NS5, OTP, PO4 NonStd Res: FME Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RCEH_BLAVI] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [CYCR_BLAVI] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. [RCEM_BLAVI] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEL_BLAVI] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. Publication Abstract from PubMed Serial crystallography is an increasingly important approach to protein crystallography that exploits both X-ray free-electron laser (XFEL) and synchrotron radiation. Serial crystallography recovers complete X-ray diffraction data by processing and merging diffraction images from thousands of randomly oriented non-uniform microcrystals, of which all observations are partial Bragg reflections. Random fluctuations in the XFEL pulse energy spectrum, variations in the size and shape of microcrystals, integrating over millions of weak partial observations and instabilities in the XFEL beam position lead to new types of experimental errors. The quality of Bragg intensity estimates deriving from serial crystallography is therefore contingent upon assumptions made while modeling these data. Here it is observed that serial femtosecond crystallography (SFX) Bragg reflections do not follow a unimodal Gaussian distribution and it is recommended that an idealized assumption of single Gaussian peak profiles be relaxed to incorporate apparent asymmetries when processing SFX data. The phenomenon is illustrated by re-analyzing data collected from microcrystals of the Blastochloris viridis photosynthetic reaction center and comparing these intensity observations with conventional synchrotron data. The results show that skewness in the SFX observations captures the essence of the Wilson plot and an empirical treatment is suggested that can help to separate the diffraction Bragg intensity from the background. Asymmetry in serial femtosecond crystallography data.,Sharma A, Johansson L, Dunevall E, Wahlgren WY, Neutze R, Katona G Acta Crystallogr A Found Adv. 2017 Mar 1;73(Pt 2):93-101. doi:, 10.1107/S2053273316018696. Epub 2017 Jan 30. PMID:28248658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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