Hugh T. Philipp

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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)
X-ray free electron lasers (XFELs) promise to revolutionize X-ray science with extremely high peak brilliances and femtosecond X-ray pulses. This will require novel detectors to fully realize the potential of these new sources. There are many current detector development projects aimed at the many challenges of meeting the XFEL requirements [1,2]. This(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)
We describe a hybrid pixel array detector (electron microscope pixel array detector, or EMPAD) adapted for use in electron microscope applications, especially as a universal detector for scanning transmission electron microscopy. The 128×128 pixel detector consists of a 500 µm thick silicon diode array bump-bonded pixel-by-pixel to an application-specific(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)
Schemes for X-ray imaging single protein molecules using new x-ray sources, like x-ray free electron lasers (XFELs), require processing many frames of data that are obtained by taking temporally short snapshots of identical molecules, each with a random and unknown orientation. Due to the small size of the molecules and short exposure times, average signal(More)
New sources and detectors are allowing scientists to look at matter with finer spatial and temporal resolutions. These experiments can produce data that are a series of severely Poisson limited snap-shots of randomly oriented samples. An extreme case of this is destructive imaging of single particles with an x-ray free-electron laser – many frames are(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)
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)
An imaging Pixel Array Detector (PAD) is being developed to record x-ray scattering images from single particles at the SLAC Linac Coherent Light Source (LCLS) x-ray free electron laser. The LCLS will deliver x-ray pulses of 5 – 200 femtosecond duration 120 times per second. Proposed experiments require that the scatter from each pulse be independently(More)