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Mechanisms, kinetics, impurities and defects: consequences in macromolecular crystallization
Author(s) -
McPherson Alexander,
Kuznetsov Yurii G.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14004816
Subject(s) - crystallization , nucleation , macromolecule , mosaicity , chemical physics , protein crystallization , crystal (programming language) , supersaturation , crystal growth , materials science , impurity , kinetics , crystallography , chemistry , nanotechnology , physics , biochemistry , epitaxy , organic chemistry , layer (electronics) , quantum mechanics , computer science , programming language
The nucleation and growth of protein, nucleic acid and virus crystals from solution are functions of underlying kinetic and thermodynamic parameters that govern the process, and these are all supersaturation‐dependent. While the mechanisms of macromolecular crystal growth are essentially the same as for conventional crystals, the underlying parameters are vastly different, in some cases orders of magnitude lower, and this produces very different crystallization processes. Numerous physical features of macromolecular crystals are of serious interest to X‐ray diffractionists; the resolution limit and mosaicity, for example, reflect the degree of molecular and lattice order. The defect structure of crystals has an impact on their response to flash‐cooling, and terminal crystal size is dependent on impurity absorption and incorporation. The variety and extent of these issues are further unique to crystals of biological macromolecules. All of these features are amenable to study using atomic force microscopy, which provides direct images at the nanoscale level. Some of those images are presented here.