Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 58, Issue -, Pages 1571-1575Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S090744490201418X
Keywords
interaction potentials; second virial coefficient; protein crystallization
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It has been shown for several years that the second virial coefficient, A(2), can be helpfully used to describe the thermodynamic behavior of biological macromolecules in solution prior to crystallization. The coefficient, which reflects either repulsive or attractive interactions between particles, can allow a rapid determination of crystallization conditions. Different biological systems, from 14 kDa to 4600 kDa, were studied by small angle Xray scattering. With large macromolecules, the A(2) values were found at the low end of the crystallization slot described by George & Wilson [(1994) Acta Cryst. D50, 361-365]. This led us to investigate the physical meaning of the second virial coefficient and to propose the use of the dimensionless second virial coefficient independent of the molecular weight and the size of the particle, which only takes into account the interaction potential between macromolecules, to predict successful crystallization conditions for large macromolecules. With this normalized coefficient (a(2)), the effect of salt on small proteins becomes equivalent to the effect of PEG on large macromolecules in terms of interaction potentials.
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