Proteins are known to undergo a dynamical transition at around 200 K but the underlying mechanism, physical origin, and relationship to water are controversial. Here we report an observation of a protein dynamical transition as low as 110 K. This unexpected protein dynamical transition precisely correlated with the cryogenic phase transition of water from a high-density amorphous to a low-density amorphous state. The results suggest that the cryogenic protein dynamical transition might be directly related to the two liquid forms of water proposed at cryogenic temperatures.

Next generation light sources are revolutionizing x-ray science by delivering ultra-intense, hard x-ray pulses many orders of magnitude brighter and shorter in duration than previously achievable. Maximizing the scientific potential of these light sources requires the development of suitable detectors. Experiments such as coherent x-ray imaging of single particles require detectors that can record extremely high instantaneous flux rates produced by femtosecond x-ray pulses (i.e.

There is growing excitement in the synchrotron materials science community about the potential of nearly diffraction-limited, high-repetition rate, hard X-ray sources, such as an Energy Recovery Linac (ERL) or an Ultimate Storage Ring (USR), and that these sources will pave the way to scientific insights and discoveries not possible with existing facilities. These future sources will deliver highly coherent, nearly diffraction-limited X-ray beams that will power ultra-intense, nanometer-scale X-ray probes and imaging capabilities approaching atomic resolution.

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 paper describes a pixel array detector (PAD) that has been developed for the Coherent X-ray Imaging experiment at the Linac Coherent Light Source (LCLS) at the SLAC National Laboratory [3].

CHESS is a hard X-ray synchrotron radiation national facility located at Cornell University and funded by the National Science Foundation. It is open to all scientists by peer-reviewed proposal and serves 5001000 visitors each year. The CHESS scientific and technical staff develops forefront research tools and X-ray instrumentation and methods and supports 12 experimental stations delivering high intensity X-ray beams produced at 5.3 GeV and 250 mA.

High-pressure methods for solving protein structures by X-ray crystallography and NMR are maturing. These techniques are beginning to impact our understanding of thermodynamic and structural features that define not only the protein's native conformation, but also the higher free energy conformations. The ability of high-pressure methods to visualize these mostly unexplored conformations provides new insight into protein function and dynamics.

A pair of techniques have been developed for performing time-resolved X-ray microdiffraction on irreversible phase transformations. In one technique capillary optics are used to focus a high-flux broad-spectrum X-ray beam to a 60 m spot size and a fast pixel array detector is used to achieve temporal resolution of μ55 s.

Solution small-angle X-ray scattering (SAXS) measurements were obtained using a 128 X 128 pixel X-ray mixed-mode pixel array detector (MMPAD) with an 860 μs readout time. The MMPAD offers advantages for SAXS experiments: a pixel full-well of >2 × 107 10 keV X-rays, a maximum flux rate of 108 X-rays pixel-1 s-1, and a sub-pixel point-spread function. Data from the MMPAD were quantitatively compared with data from a charge-coupled device (CCD) fiber-optically coupled to a phosphor screen.

Dynamic X-ray studies can reach temporal resolutions limited by only the X-ray pulse duration if the detector is fast enough to segregate synchrotron pulses. An analog integrating pixel array detector with in-pixel storage and temporal resolution of around 150 ns, sufficient to isolate pulses, is presented. Analog integration minimizes count-rate limitations and in-pixel storage captures successive pulses. Fundamental tests of noise and linearity as well as high-speed laser measurements are shown.

Mesoporous silica with cubic symmetry has attracted interest from researchers for some time. Here, we present the room temperature synthesis of mesoporous silica nanoparticles possessing cubic Pm3?n symmetry with very high molar ratios (>50%) of 3-aminopropyl triethoxysilane. The synthesis is robust allowing, for example, co-condensation of organic dyes without loss of structure. By means of pore expander molecules, the pore size can be enlarged from 2.7 to 5 nm, while particle size decreases.