When metals are cooled, they often undergo a phase transition to a state exhibiting a new
type of order. Metals such as iron and nickel become ferromagnetic below temperatures of …

10.7554/eLife.07574.001 Determining the interconverting conformations of dynamic proteins
in atomic detail is a major challenge for structural biology. Conformational heterogeneity in …

Vitrification of aqueous cryoprotectant mixtures is essential in cryopreservation of proteins
and other biological samples. Systematic measurements of critical cryoprotective agent (CPA) …

A series of studies that provide a consistent and illuminating picture of global radiation
damage to protein crystals, especially at temperatures above ∼200 K, are described. The …

Ice formation on warming is of comparable or greater importance to ice formation on cooling
in determining survival of cryopreserved samples. Critical warming rates required for ice-…

The dependence of radiation damage to protein crystals at cryogenic temperatures upon
the X-ray absorption cross-section of the crystal has been examined. Lysozyme crystals …

We study how the microscale topography of a solid surface affects the apparent advancing
and receding angles at the contact line of a liquid drop pinned to this surface. …

Small angle x-ray scattering (SAXS) is a versatile and widely used technique for obtaining
low-resolution structures of macromolecules and complexes. SAXS experiments measure …

Small-angle X-ray scattering (SAXS) is an increasingly popular technique that provides low-resolution
structural information about biological macromolecules in solution. Many of the …

The temperature-dependence of radiation damage to thaumatin crystals between T = 300
and 100 K is reported. The amount of damage for a given dose decreases sharply as the …