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6MH8

High-viscosity injector-based Pink Beam Serial Crystallography of Micro-crystals at a Synchrotron Radiation Source

Summary for 6MH8
Entry DOI10.2210/pdb6mh8/pdb
DescriptorAdenosine receptor A2a, Soluble cytochrome b562 chimeric construct, 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol (2 entities in total)
Functional Keywordsgpcr, pink beam serial crystallography, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains1
Total formula weight50311.62
Authors
Primary citationMartin-Garcia, J.M.,Zhu, L.,Mendez, D.,Lee, M.Y.,Chun, E.,Li, C.,Hu, H.,Subramanian, G.,Kissick, D.,Ogata, C.,Henning, R.,Ishchenko, A.,Dobson, Z.,Zhang, S.,Weierstall, U.,Spence, J.C.H.,Fromme, P.,Zatsepin, N.A.,Fischetti, R.F.,Cherezov, V.,Liu, W.
High-viscosity injector-based pink-beam serial crystallography of microcrystals at a synchrotron radiation source.
Iucrj, 6:412-425, 2019
Cited by
PubMed Abstract: Since the first successful serial crystallography (SX) experiment at a synchrotron radiation source, the popularity of this approach has continued to grow showing that third-generation synchrotrons can be viable alternatives to scarce X-ray free-electron laser sources. Synchrotron radiation flux may be increased ∼100 times by a moderate increase in the bandwidth ('pink beam' conditions) at some cost to data analysis complexity. Here, we report the first high-viscosity injector-based pink-beam SX experiments. The structures of proteinase K (PK) and A adenosine receptor (AAR) were determined to resolutions of 1.8 and 4.2 Å using 4 and 24 consecutive 100 ps X-ray pulse exposures, respectively. Strong PK data were processed using existing Laue approaches, while weaker AAR data required an alternative data-processing strategy. This demonstration of the feasibility presents new opportunities for time-resolved experiments with microcrystals to study structural changes in real time at pink-beam synchrotron beamlines worldwide.
PubMed: 31098022
DOI: 10.1107/S205225251900263X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.2 Å)
Structure validation

237423

数据于2025-06-11公开中

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