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Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from(More)
The production of high-performance carbon nanotube (CNT) materials demands understanding of the growth behavior of individual CNTs as well as collective effects among CNTs. We demonstrate the first use of grazing incidence small-angle X-ray scattering to monitor in real time the synthesis of CNT films by chemical vapor deposition. We use a custom-built(More)
Coherent (X-ray) diffractive imaging (CDI) is an increasingly popular form of X-ray microscopy, mainly due to its potential to produce high-resolution images and the lack of an objective lens between the sample and its corresponding imaging detector. One challenge, however, is that very high dynamic range diffraction data must be collected to produce both(More)
Single-particle imaging experiments of biomolecules at x-ray free-electron lasers (XFELs) require processing hundreds of thousands of images that contain very few x-rays. Each low-fluence image of the diffraction pattern is produced by a single, randomly oriented particle, such as a protein. We demonstrate the feasibility of recovering structural(More)
X-ray free-electron lasers (XFELs) have inspired the development of serial femtosecond crystallography (SFX) as a method to solve the structure of proteins. SFX datasets are collected from a sequence of protein microcrystals injected across ultrashort X-ray pulses. The idea behind SFX is that diffraction from the intense, ultrashort X-ray pulses leaves the(More)
A wide-dynamic-range imaging X-ray detector designed for recording successive frames at rates up to 10 MHz is described. X-ray imaging with frame rates of up to 6.5 MHz have been experimentally verified. The pixel design allows for up to 8-12 frames to be stored internally at high speed before readout, which occurs at a 1 kHz frame rate. An additional mode(More)
X-ray serial microcrystallography involves the collection and merging of frames of diffraction data from randomly oriented protein microcrystals. The number of diffracted X-rays in each frame is limited by radiation damage, and this number decreases with crystal size. The data in the frame are said to be sparse if too few X-rays are collected to determine(More)
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