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Control of nucleation and growth in protein crystal growth

Published on Jul 1, 1988in Journal of Crystal Growth1.573
· DOI :10.1016/0022-0248(88)90300-4
Franz Rosenberger30
Estimated H-index: 30
(UAH: University of Alabama in Huntsville),
Edward J. Meehan16
Estimated H-index: 16
(UAH: University of Alabama in Huntsville)
Abstract
The potential advantages of nucleation and growth control through temperature, rather than the addition of precipitants or removal of solvent, are discussed. A simple light scattering arrangement for the characterization of nucleation and growth conditions in solutions is described. The temperature dependence of the solubility of low ionic strength lysozyme solutions is applied in preliminary nucleation and growth experiments.
  • References (17)
  • Citations (43)
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#1Sandra B. Howard (UAH: University of Alabama in Huntsville)H-Index: 6
#2Pamela J. Twigg (UAH: University of Alabama in Huntsville)H-Index: 3
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Abstract The equilibrium solubility of chicken egg-white lysozyme in the presence of crystalline solid state was determined as a function of NaCl concentration, pH, and temperature. The solubility curves obtained represent a region of the lysozyme phase diagram. This diagram makes it possible to determine the supersaturation of a given set of conditions or to achieve identical supersaturations by different combinations of parameters. The temperature dependence of the solubility permits the evalu...
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Abstract Colloid stability theory has been applied to protein crystallization and predicts a narrow range of conditions under which crystals can be grown without the agglomeration of protein molecules (colloids) in the bulk solution. It also predicts a critical electrolyte concentration above which agglomeration will always occur. Using this theory, the rapid protein agglomeration occurring during Schlieren experiments as well as a terminal crystal size effect in a fixed container were explained...
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#1William W. Fowlis (MSFC: Marshall Space Flight Center)H-Index: 8
#2Lawrence J. DeLucas (UAB: University of Alabama at Birmingham)H-Index: 25
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Abstract In the hanging drop method of protein crystal growth, a water droplet containing protein, buffer and a precipitating agent, such as ammonium sulfate, is suspended from a glass coverslip above a well containing an aqueous solution of the precipitating agent at a concentration double that in the drop. We present a comprehensive theoretical study of the rate of water evaporation in the hanging drop method. We find that in earth's gravity the rate controlling step in the evaporation is the ...
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Abstract Crystallographic studies of biological macromolecules have proved of great value in establishing the structural foundations of biochemistry and molecular biology, and for revealing structure/function relationships that are of importance in our understanding of how enzymes, nucleic acids, and other macromolecules operate in biological systems. There have been major advances in the technology involved in determining protein crystal structures, once suitable crystals are available. The maj...
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Abstract Transport and interface kinetics concepts that have proven successful in the design and control of inorganic crystal growth experiments are outlined. Their potential usefulness and limitations in protein crystal growth are discussed. The presentation follows a selection of observations and statements that are often made by workers in the protein crystal growth field. The paper is meant to be tutorial in nature. Emphasis is placed on concepts which bear practical significance. Though the...
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Abstract Protein crystal growth in space is of interest because of the potential applications for unique studies of crystallization processes. Theoretical and experimental research indicates that gravitational fields produce density-driven convective flow patterns which can influence crystal growth, and these convective effects can be controlled under microgravity conditions. Microgravity can also be used to control sedimentation effects. As part of a program to investigate the influence of grav...
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Abstract The nucleation and growth of a model protein, lysozyme, was investigated. Theoretical models were developed and checked against experimental results.
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#1Walter Littke (University of Freiburg)H-Index: 6
#2Christina John (University of Freiburg)H-Index: 3
Abstract Crystal growth conditions for proteins under microgravity were investigated with two model compounds (β-galactosidase and lysozyme). The single crystals obtained have been found to be significantly larger than those prepared in the same environment on earth.
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#2N. V. Krivonogova (RAS: Russian Academy of Sciences)H-Index: 1
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Abstract Two techniques for the nucleation and growth of single crystals of biological macromolecules are proposed. The first one utilizes a very slow temperature shift at a capillary point where the crystal is to be grown. This allows to suppress an undesirable multiple nucleation. The second technique includes several local rapid temperature changes (a temperature “shock”) forcing the nucleation at the given point. These techniques were successfully tested while growing single crystals of lyso...
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#1Yun Guo (TJU: Tianjin University)H-Index: 2
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Abstract The binding domains of lysozyme with ionic liquids (ILs, [C4mim]BF4, [C4mim]Cl, [C4mim]Br and [dmim]I) in aqueous solution was investigated by studying molecular interactions using spectroscopic techniques. Ultraviolet spectroscopy (UV) showed that the addition of ILs increased the absorption peak intensity of lysozyme at 210 nm by enhancing peptide bond valence electron transition. It is also found that a weak interaction between ILs and lysozyme chromophore groups was generated by ana...
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#1Mike Sleutel (Vrije Universiteit Brussel)H-Index: 12
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Macromolecular phase transitions bear great medical, scientific and industrial relevance, yet the molecular picture of their earliest beginnings is still far from complete. For decades, progress has been hampered by the challenges associated with studying stochastic nucleation phenomena occurring on nanoscopic length scales. In the last 5 years, however, the field has advanced with great strides due to the recent buildout of experimental techniques that allow us to observe details of the nucleat...
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#1V. V. Safronov (RAS: Russian Academy of Sciences)H-Index: 2
#2N. V. Krivonogova (RAS: Russian Academy of Sciences)H-Index: 1
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A technique of temperature-controlled biocrystal nucleation, at which the growth onset of one crystal suppresses the development of other nuclei, is proposed. This is obtained by decreasing gradually the temperature at the point of expected growth at a rate sufficiently low to equalize the protein concentration (under conditions where material is captured by growing crystal) via diffusive and convective processes. An individual growth of lysozyme single crystals in a capillary is demonstrated.
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Protein crystals have many important applications in many fields, including pharmaceutics. Being more stable than other formulations, and having a high degree of purity and bioavailability, they are especially promising in the area of drug delivery. In this contribution, the development of a continuously operated tubular crystallizer for the production of protein crystals has been described. Using the model enzyme lysozyme, we successfully generated product particles ranging between 15 and 40 μm...
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The thermal variant of the classical nucleation-growth-separation principle is shown, both theoretically and experimentally, to be a reliable tool for studying protein crystal nucleation. The classical nucleation theory is used to elucidate the temperature dependence of crystal nucleus size. A one-to-one ratio of the number density of nuclei formed to crystals grown to visible size is achieved using the nucleation-growth-separation method. The experiments conducted in such a way show that new nu...
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