Lysozyme solubility in H2O and D2O solutions: a simple relationship

Gripon, C.; Legrand, Laurent; Rośenman, I.; Vidal, O.; Robert, M.C.; Boué, François

doi:10.1016/s0022-0248(96)01077-9

Cited by 49 publications

(50 citation statements)

References 25 publications

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“…1) Neal et al, 1998;Tessier & Lenhoff, 2003;Bonneté & Vivarè s, 2002;Demoruelle et al, 2002;Ruppert et al, 2001). An empirical correlation between B (a dilute solution parameter) and the solubility s (a phase-transition parameter) has also been demonstrated for several proteins (Demoruelle et al, 2002;Gripon et al, 1997;Guo et al, 1999).…”

Section: Reviewmentioning

confidence: 86%

“…However, the application of ANN and incomplete factorial solubility screens has proven to be more promising. The correlation between B and protein solubility has been presented both experimentally and theoretically for several proteins (Demoruelle et al, 2002;Gripon et al, 1997;Haas et al, 1999;Malfois et al, 1996;Neal et al, 1998;Ruppert et al, 2001). Fig.…”

Section: Figurementioning

confidence: 99%

See 1 more Smart Citation

Applications of the second virial coefficient: protein crystallization and solubility

Wilson

DeLucas

2014

Acta Crystallogr F Struct Biol Commun

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This article begins by highlighting some of the ground-based studies emanating from NASA's Microgravity Protein Crystal Growth (PCG) program. This is followed by a more detailed discussion of the history of and the progress made in one of the NASA-funded PCG investigations involving the use of measured second virial coefficients (Bvalues) as a diagnostic indicator of solution conditions conducive to protein crystallization. A second application of measuredBvalues involves the determination of solution conditions that improve or maximize the solubility of aqueous and membrane proteins. These two important applications have led to several technological improvements that simplify the experimental expertise required, enable the measurement of membrane proteins and improve the diagnostic capability and measurement throughput.

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Section: Reviewmentioning

confidence: 86%

Section: Figurementioning

confidence: 99%

Applications of the second virial coefficient: protein crystallization and solubility

Wilson

DeLucas

2014

Acta Crystallogr F Struct Biol Commun

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“…They were brought to supersaturation by adding NaCI to a final concentration of ~ 1998 International Union of ('rystallography Printed in Great Britain -all rights reserved 6% (w/v). Experimental data reported in the literature (Howard et al, 1988: Gripon et al, 1997 indicate a solubility of 4-6 mg ml-~ for lysozymc in an aqueous solution with 6% NaCI and pH 4.7 in the temperature range 293-303 K. The effect of D20 on the solubility is small (Gripon et al. 1997).…”

Section: Methodsmentioning

confidence: 98%

Nucleation in Protein Crystallization

Drenth

Haas

1998

Acta Crystallogr D Biol Crystallogr

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In this paper protein crystallization is regarded as a process starting with phase separation in a twocomponent system. The nucleation time of a lysozyme solution is measured by recording the NMR spectra of crystallizing solutions as a function of time. It is found that there is an appreciable induction time before the first nuclei appear in the solution and that this induction time depends strongly on the degree of supersaturation owing to the protein concentration at a given ionic strength or owing to the temperature. From the experimental data it is evident that (at least for lysozymc) crystallization under the prevailing experimental conditions is a transient process with an induction time and not a steady-state process.

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“…The sample is then installed in a temperature controlled sample holder and undergoes a temperature sweep (0.6 degree/hour) while stirring to maintain the microcrystallites in suspension (Rosenberger et al, 1993;Gripon et al, 1997). The intensity of a red laser light scattered at 90°is recorded and drops rapidly to zero when the crystallites dissolve.…”

Section: Light Detection Methodsmentioning

confidence: 99%

“…Many more lysozyme solubility measurements have been devoted to the tetragonal and orthorhombic forms (see for example Ataka & Asai, 1988;Howard et al, 1988;Riès-Kautt & Ducruix, 1989;Cacioppo & Pusey, 1991;Elgersma et al, 1992;Guilloteau et al,1992;Rosenberger et al, 1993;Gripon et al, 1997;Retailleau et al, 1997;Bénas et al, 2002) than to the monoclinic and triclinic ones (Riès-Kautt & Ducruix, 1989;Guilloteau et al, 1992;Retailleau, 1996;Legrand et al, 2001;Retailleau, 2002). The temperature dependence of the triclinic form has not been quantified so far by solubility measurements.…”

Section: Introductionmentioning

confidence: 99%

Two polymorphs of lysozyme nitrate: temperature dependence of their solubility

Legrand¹,

Riès-Kautt²,

Robert³

2002

Acta Crystallogr D Biol Cryst

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Two crystallographic forms of lysozyme nitrate are known, namely monoclinic and triclinic. Having previously determined the temperature dependence of the solubility of the monoclinic form (0.2 M NaNO 3 solutions at pH = 4.5) [Legrand et al. (2001). J. Cryst. Growth, 232, 244-249], we focus here on the solubility of the triclinic form. The temperature dependence of the solubility of this crystallographic form has been measured with a static light device developed in our laboratory. This device allows to observe of the dissolution of one phase and/or the occurrence of a new one by varying the temperature with a sweep rate as low as 0.6 degree/hour. The new solubility data are complemented with crystallographic data of the triclinic form for the sake of completeness. The faces of a triclinic crystal are indexed. The crystallisation enthalpy of the triclinic form is deduced from these new results. These new solubility data allow us now to discuss (1) the publishedprotocols used to obtain the monoclinic and triclinic forms of lysozyme nitrate and (2) the phase transformation.

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Lysozyme solubility in H2O and D2O solutions: a simple relationship

Cited by 49 publications

References 25 publications

Applications of the second virial coefficient: protein crystallization and solubility

Applications of the second virial coefficient: protein crystallization and solubility

Nucleation in Protein Crystallization

Two polymorphs of lysozyme nitrate: temperature dependence of their solubility

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