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A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging‐ and sitting‐drop vapor‐diffusion and microdialysis experiments
Author(s) -
Luft J. R.,
Arakali S. V.,
Kirisits M. J.,
Kalenik J.,
Wawrzak I.,
Cody V.,
Pangborn W. A.,
DeTitta G. T.
Publication year - 1994
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889893012713
Subject(s) - diffusion , crystallization , drop (telecommunication) , macromolecule , microdialysis , materials science , chemistry , chemical engineering , chemical physics , thermodynamics , physics , engineering , organic chemistry , mechanical engineering , biochemistry , extracellular
A procedure and crystallization plate are described that allow control over the time course of equilibration between a macromolecule and a reservoir solution. The d 2 dependence of diffusion is exploited in a crystallization plate with reservoirs of varying depths to speed up or slow down the equilibration. A rationale is presented that suggests why this might be useful. The plate is a completely passive device, with no moving parts, that can be set up in about the same time as a traditional 24‐well plate. It can, with equal facility, be used for hanging‐drop or sitting‐drop vapor diffusion or microdialysis crystallization experiments. The procedure has been used to grow very large diffraction‐quality crystals of three protein‐inhibitor complexes, one of which had failed to yield any but microcrystals by more traditional methods.