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References (10)
-
W. Fredericks, M. Hammonds, S. Howard, F. Rosenberger (1994)
Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrationsJournal of Crystal Growth, 141
-
E. Garman, T. Schneider, Rabinovich Joshua-Tor, F. Hope (1997)
Macromolecular Cryocrystallography -
(1943)
The interactions of proteins with ions and dipolar ions -
G. Gilliland (1988)
A biological macromolecule crystallization database: A basis for a crystallization strategyJournal of Crystal Growth, 90
-
Tzu-Ping Ko, J. Day, A. Greenwood, Alexander McPherson (1994)
Structures of three crystal forms of the sweet protein thaumatin.Acta crystallographica. Section D, Biological crystallography, 50 Pt 6
-
(1994)
Distance between protein molecules in solution -
(1999)
Protein Crystallization International University Line -
Kim Collins, Michael Washabaugh (1985)
The Hofmeister effect and the behaviour of water at interfacesQuarterly Reviews of Biophysics, 18
-
K. Collins (1995)
Sticky ions in biological systems.Proceedings of the National Academy of Sciences of the United States of America, 92 12
-
I. Smatanova (1997)
Crystallization of Biological Macromolecules
- Publisher
- Wiley
- Copyright
- Copyright © 2001 The Protein Society
- ISSN
- 0961-8368
- eISSN
- 1469-896X
- DOI
- 10.1110/ps.32001
- pmid
- 11266627
- Publisher site
- See Article on Publisher Site
Abstract
Thirty‐one proteins and viruses that we knew from our own experience could be crystallized, or had been reported to have been crystallized by others, were investigated. In this experiment, each protein or virus was subjected to a crystallization screen of 12 different salts, each titrated to pH 7.2 beforehand, at concentrations ranging from 20% saturation to 90% saturation. Eight macromolecules failed to crystallize at all from any salt and were omitted from consideration. From the remaining 23 proteins, each salt was scored according to how many proteins and viruses it successfully crystallized. Among several results, one was particularly striking. Sodium malonate clearly was much more successful than any other salt, resulting in the crystallization of 19 of the 23 macromolecules, almost twice as effective as the next most successful salt, which was a draw between sodium acetate, sodium tartrate, sodium formate, and ammonium sulfate (11 of 22). The high success rate of sodium malonate in producing crystals was even more impressive when an overall unique success rate with individual macromolecules was considered.
Journal
Protein Science – Wiley
Published: Feb 1, 2001