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5A45

Structure of Bacteriorhodopsin obtained from 5um crystals by multi crystal data collection

Summary for 5A45
Entry DOI10.2210/pdb5a45/pdb
Related5A3Y 5A3Z 5A44 5A47
DescriptorBACTERIORHODOPSIN, RETINAL (2 entities in total)
Functional Keywordsproton transport, multi crystal data collection, synchrotron serial crystallography, membrane protein, lcp, ssx, ion pump, retinal protein, photoreceptor, 7-helix transmembrane, ion transport
Biological sourceHALOBACTERIUM SALINARUM
Cellular locationCell membrane; Multi-pass membrane protein: P02945
Total number of polymer chains1
Total formula weight27098.85
Authors
Zander, U.,Bourenkov, G.,Popov, A.N.,de Sanctis, D.,McCarthy, A.A.,Svensson, O.,Round, E.S.,Gordeliy, V.I.,Mueller-Dieckmann, C.,Leonard, G.A. (deposition date: 2015-06-05, release date: 2015-11-11, Last modification date: 2024-11-20)
Primary citationZander, U.,Bourenkov, G.,Popov, A.N.,De Sanctis, D.,Svensson, O.,Mccarthy, A.A.,Round, E.,Gordeliy, V.,Mueller-Dieckmann, C.,Leonard, G.A.
Meshandcollect: An Automated Multi-Crystal Data-Collection Workflow for Synchrotron Macromolecular Crystallography Beamlines.
Acta Crystallogr.,Sect.D, 71:2328-, 2015
Cited by
PubMed Abstract: Here, an automated procedure is described to identify the positions of many cryocooled crystals mounted on the same sample holder, to rapidly predict and rank their relative diffraction strengths and to collect partial X-ray diffraction data sets from as many of the crystals as desired. Subsequent hierarchical cluster analysis then allows the best combination of partial data sets, optimizing the quality of the final data set obtained. The results of applying the method developed to various systems and scenarios including the compilation of a complete data set from tiny crystals of the membrane protein bacteriorhodopsin and the collection of data sets for successful structure determination using the single-wavelength anomalous dispersion technique are also presented.
PubMed: 26527148
DOI: 10.1107/S1399004715017927
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.57 Å)
Structure validation

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