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We demonstrate that powder diffraction data can be collected from sub-microncrystals of a mbrane protein with nearly two orders of magnitude more atomsthan the molecules commonly used for powder diffraction. The crystals ofphotosystem-1 protein were size-selected using a 500 nm pore- size filter anddelivered to a soft x-ray beam with a photon energy of 1.5 keV using adynamically focused micro-jet developed for the serial crystallographyexperiment at beamline 9.0.1. The 10-micron jet places many such randomlyoriented crystals in the x-ray beam simultaneously resulting in a powderdiffraction pattern which extends to 28 angstrom resolution with just 200seconds of x-ray exposure. The use of the jet for particle delivery allows fora thin sample, appropriate for the soft x-rays used, and continuously refreshesthe crystals so that radiation damage is not possible. The small size of thecrystals requires the use of lower energy photons for increased scatteringstrength and increased spacing between powder rings. The powder patternsobtained in this way, from abundant nano-crystals, could be used to provide lowresolution molecular envelopes if phased using techniques such as compressivesensing which do not require atomic resolution data. The results also serve totest our aerojet injector system, with future application to femtoseconddiffraction in Free Electron X-ray Laser schemes, and for SerialCrystallography using a single-file beam of aligned hydrated molecules.

X-Ray Powder Diffraction from Sub-Micron Crystals of Photosystem-1 Membrane Protein