Slow evaporation of the reservoir in microdialysis can lead to a significant increase in the crystal size of proteins for which the crystallization region of supersaturation is particularly limited.

A helium cryostat developed at the University of Toledo has been used to flash-cool and collect data from crystals of lysozyme and myoglobin, including flash-cooled crystals large enough for neutron diffraction purposes. The liquid-He consumption of the device is sufficiently low to allow the acquisition of complete diffraction data from a crystal on a single tank of He, and should expand He-temperature data-collection opportunities.