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Figure 2
Bragg diffraction at sub-nanometer resolution from membrane protein 2-D crystals. (a) Background-subtracted diffraction patterns for 2-D crystals of bacteriorhodopsin. Blue circles signify resolution rings at 30.0, 15.0 and 7.5 Å (inner to outer). The zoomed-in red circle highlights the peaks with highest resolution at 8.5 and 8.7 Å, (h, k) = (2, 5) and (3, 4), respectively. The diffraction patterns were acquired with a sample-to-detector distance of 340 mm and a photon energy of 8448 eV. (b) Experimental 2-D electron density projection map (2 × 2 unit cells) from coupling the observed integrated peak intensities with the corresponding calculated phases from the known crystal structure of bacteriorhodopsin. (c) Ribbon diagram (2 × 2 unit cells) of bacteriorhodopsin created using the known crystal structure, symmetry and unit cell for comparison with (b). The scale bar is equivalent for panels (b) and (c).

IUCrJ
Volume 1| Part 2| February 2014| Pages 95-100
ISSN: 2052-2525
doi:10.1107/S2052252514001444