Controlling nucleation in protein solutions

DeMattei, R.C.; Feigelson, Robert S.

doi:10.1016/0022-0248(92)90222-5

Cited by 32 publications

(24 citation statements)

References 3 publications

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“…The technique of varying the temperature is beginning to show great promise (see for example DeMattei & Feigelson, 1992;Lorber & Geige Â, 1992;Schall et al, 1996). The goal is to lower the degree of supersaturation just before many nuclei cross the energy barrier and become stable micro-crystals, thereby preventing all but one or a few nuclei from becoming stable.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, there have been efforts to control nucleation through means such as varying the temperature (Rosenberger & Meehan, 1988) and varying the precipitant concentration (Blow et al, 1994) as functions of time. The technique of varying the temperature is beginning to show great promise (see for example DeMattei & Feigelson, 1992;Lorber & Geige Â, 1992;Schall et al, 1996). The goal is to lower the degree of supersaturation just before many nuclei cross the energy barrier and become stable micro-crystals, thereby preventing all but one or a few nuclei from becoming stable.…”

Section: Introductionmentioning

confidence: 99%

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An accurate numerical model for calculating the equilibration rate of a hanging-drop experiment

Diller¹,

Hól²

1999

Acta Crystallogr D Biol Cryst

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A numerical model of the equilibration of a hanging-drop experiment has been developed and tested. To obtain accurate calculations with a given precipitant, the vapor pressure of water over water/precipitant solutions must be known for various concentrations of the precipitant. The calculations of the model are in excellent agreement with all available experimental data on hanging-drop equilibration when the necessary vapor pressures are known (ammonium sulfate and sodium chloride). By varying each of the relevant rate constants in the model, the rate-limiting step in the equilibration of a hanging drop is determined. This analysis clearly shows that the rate-limiting step is the diffusion of water vapor from the drop to the reservoir, which agrees with experimental ®ndings. Since the diffusion of water vapor is the rate-limiting step, there is virtually no precipitant concentration gradient in the drop during equilibration. As a result, there is no gravity-induced convection owing to the equilibration. Thus, whereas gravity might have an effect during crystal growth, gravity does not affect the equilibration rate of a hanging-drop experiment to a signi®cant extent, and the diffusion of water vapor will remain the rate-limiting step in the absence of gravity. Finally, the effects of several of the parameters, such as initial drop volume, drop-to-reservoir distance and temperature, are considered quantitatively. The equilibration rate was found to vary nearly linearly with drop volume. The equilibration rate decreases roughly by a factor of three as the temperature decreases from 293 to 276 K. This decrease in the equilibration rate is greater than would be expected when just considering the change in the diffusion coef®cient of water vapor in air. This large dependence can, however, be attributed to the change in water-vapor pressure. Most surprisingly, a linear dependence on drop-to-reservoir distance is found, a result that agrees very well with experiment.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An accurate numerical model for calculating the equilibration rate of a hanging-drop experiment

Diller¹,

Hól²

1999

Acta Crystallogr D Biol Cryst

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“…It was thus possible to make a calibration of the X-ray properties of ground-grown crystals to compare them with spacegrown ones using identical conditions except the level of gravity. The reasons for the choice of hen egg-white lysozyme as a model protein were multiple: the structure of lysozyme is known at high resolution (Madhusudan, Kodandapani & Vijayan, 1993;Harata, 1994;Pike & Acharya, 1994;Kurinov & Harrison, 1995), it is easily available in gram quantities, it crystallizes in a time span compatible with the duration of a US Shuttle flight, its phase diagram on earth is known at various temperatures (Ataka & Asai, 1988;Howard, Twigg, Baird & Meehan, 1988;Guilloteau, Ri~s-Kautt & Ducruix, 1992), and it is one of the most extensively studied proteins in crystallogenesis (Feher & Kam, 1985;Ataka & Asai, 1988;Ri~s-Kautt & Ducruix, 1989;Mikol, Hirsch & Giegr, 1990;DeMattei & Feigelson, 1992;Monaco & Rosenberger, 1993;Forsythe & Pusey, 1994).…”

Section: Introductionmentioning

confidence: 99%

High-Resolution Structure (1.33 Å) of a HEW Lysozyme Tetragonal Crystal Grown in the APCF Apparatus. Data and Structural Comparison with a Crystal Grown under Microgravity from SpaceHab-01 Mission

Vaney¹,

Maignan²,

Riès-Kautt³

et al. 1996

Acta Crystallogr D Biol Crystallogr

296

264

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Crystals of tetragonal hen egg-white lysozyme were grown using Advanced Protein Crystallization Facility (APCF) apparatus under a microgravity environment (SpaceHab-01 mission) and ground control conditions. Crystals were grown from NaCI as a crystallizing agent at pH 4.3. The X-ray diffraction patterns of the best diffracting ground-and space-grown crystals were recorded using synchrotron radiation and an image plate on the W32 beamline at LURE. Both ground-and space-grown crystals showed nearly equivalent maximum resolution of 1.3-1.4,~. Refinements were carried out with the program X-PLOR with final R values of 18.45 and 18.27% for structures from ground-and spacegrown crystals, respectively. The two structures are nearly identical with the root-mean-square difference on all protein atoms being 0.13/~. Some residues of the two refined structures show multiple alternative conformations. Two ions were localized into the electron-density maps of the two structures: one chloride ion at the interface between two symmetry-related molecules and one sodium ion stabilizing the loop Ser60-Leu75. The sodium ion is surrounded by six ligands which form a bipyramid around it at distances of 2.2-2.6 A,.

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“…An alternative possibility would be to stimulate protein nucleation by temperature or ultrasounds, as demonstrated for small molecules [157]. This was achieved in the 1990s for temperature [158] and, more recently, for ultrasound waves [159] (Table 6).…”

Section: Nucleation and Growthmentioning

confidence: 99%

A historical perspective on protein crystallization from 1840 to the present day

Giegé

2013

FEBS J

106

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Protein crystallization has been known since 1840 and can prove to be straightforward but, in most cases, it constitutes a real bottleneck. This stimulated the birth of the biocrystallogenesis field with both ‘practical’ and ‘basic’ science aims. In the early years of biochemistry, crystallization was a tool for the preparation of biological substances. Today, biocrystallogenesis aims to provide efficient methods for crystal fabrication and a means to optimize crystal quality for X‐ray crystallography. The historical development of crystallization methods for structural biology occurred first in conjunction with that of biochemical and genetic methods for macromolecule production, then with the development of structure determination methodologies and, recently, with routine access to synchrotron X‐ray sources. Previously, the identification of conditions that sustain crystal growth occurred mostly empirically but, in recent decades, this has moved progressively towards more rationality as a result of a deeper understanding of the physical chemistry of protein crystal growth and the use of idea‐driven screening and high‐throughput procedures. Protein and nucleic acid engineering procedures to facilitate crystallization, as well as crystallization methods in gelled‐media or by counter‐diffusion, represent recent important achievements, although the underlying concepts are old. The new nanotechnologies have brought a significant improvement in the practice of protein crystallization. Today, the increasing number of crystal structures deposited in the Protein Data Bank could mean that crystallization is no longer a bottleneck. This is not the case, however, because structural biology projects always become more challenging and thereby require adapted methods to enable the growth of the appropriate crystals, notably macromolecular assemblages.

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Controlling nucleation in protein solutions

Cited by 32 publications

References 3 publications

An accurate numerical model for calculating the equilibration rate of a hanging-drop experiment

An accurate numerical model for calculating the equilibration rate of a hanging-drop experiment

High-Resolution Structure (1.33 Å) of a HEW Lysozyme Tetragonal Crystal Grown in the APCF Apparatus. Data and Structural Comparison with a Crystal Grown under Microgravity from SpaceHab-01 Mission

A historical perspective on protein crystallization from 1840 to the present day

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