 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](ic5093fig3mag.jpg)
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Figure 3
Diffraction tests of rhodopsin microcrystals at the SLS synchrotron and at the X-ray free-electron laser (XFEL). At the synchrotron, powder diffraction of a pellet of rhodopsin crystals kept at room temperature in the dark (a) or for 5 min in white light (b) was performed on the PXIII beamline of the SLS (5 keV, 10 s exposure). Diffraction rings are visible up to ∼9 Å resolution. After illumination, the pellet turned from red [inset in (a); retinal chromophore in the cis conformation] to yellow [inset in (b); retinal in the trans conformation], the crystals became disordered and the diffraction disappeared (b). At the XFEL, the rhodopsin crystals were tested on the CXI beamline of the LCLS at SLAC using a liquid jet. (c) shows a virtual powder diffraction pattern obtained by merging 2186 `hits' extending to a resolution of 4–5 Å. This powder pattern shows an anisotropic distribution of Bragg peaks, which could reflect a preferred orientation of the crystals in the liquid stream. |
![[Figure 3]](ic5093fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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