Protein crystallizations. The functional dependence of the nucleation rate on the protein concentration and the solubility

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Abstract

Crystallization of proteins is normally carried out in a four-component system of water, a buffer, protein and precipitant, either salt or alcohol. With four components, at fixed pH, temperature and pressure, it is possible to vary the protein concentration and its solubility independently, because the solubility is determined by the precipitant concentration. This degree of freedom is useful in crystallizing rabbit muscle aldolase and lysozyme because the nucleation rate is a function only of the total protein concentration and not of the protein solubility. Large crystals are obtained when both the protein concentration and the protein solubility are small. The small protein concentration suppresses the rate of nucleation, and the small solubility provides sufficient protein to grow large crystals on the few nuclei. Sometimes it is desirable to grow crystals from seeds, especially if a special crystal form is required. In this case also, homogeneous nucleation of an unfavorable form may be avoided for aldolase through the use of low protein concentration.

Original languageEnglish (US)
Pages (from-to)139-144
Number of pages6
JournalJournal of Crystal Growth
Volume44
Issue number2
DOIs
StatePublished - 1978

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Crystallization
Nucleation
solubility
Solubility
nucleation
crystallization
proteins
Proteins
aldolase
Fructose-Bisphosphate Aldolase
Crystals
crystals
rabbits
lysozyme
Muramidase
muscles
Seed
Muscle
seeds
Buffers

ASJC Scopus subject areas

  • Condensed Matter Physics

Cite this

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abstract = "Crystallization of proteins is normally carried out in a four-component system of water, a buffer, protein and precipitant, either salt or alcohol. With four components, at fixed pH, temperature and pressure, it is possible to vary the protein concentration and its solubility independently, because the solubility is determined by the precipitant concentration. This degree of freedom is useful in crystallizing rabbit muscle aldolase and lysozyme because the nucleation rate is a function only of the total protein concentration and not of the protein solubility. Large crystals are obtained when both the protein concentration and the protein solubility are small. The small protein concentration suppresses the rate of nucleation, and the small solubility provides sufficient protein to grow large crystals on the few nuclei. Sometimes it is desirable to grow crystals from seeds, especially if a special crystal form is required. In this case also, homogeneous nucleation of an unfavorable form may be avoided for aldolase through the use of low protein concentration.",
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N2 - Crystallization of proteins is normally carried out in a four-component system of water, a buffer, protein and precipitant, either salt or alcohol. With four components, at fixed pH, temperature and pressure, it is possible to vary the protein concentration and its solubility independently, because the solubility is determined by the precipitant concentration. This degree of freedom is useful in crystallizing rabbit muscle aldolase and lysozyme because the nucleation rate is a function only of the total protein concentration and not of the protein solubility. Large crystals are obtained when both the protein concentration and the protein solubility are small. The small protein concentration suppresses the rate of nucleation, and the small solubility provides sufficient protein to grow large crystals on the few nuclei. Sometimes it is desirable to grow crystals from seeds, especially if a special crystal form is required. In this case also, homogeneous nucleation of an unfavorable form may be avoided for aldolase through the use of low protein concentration.

AB - Crystallization of proteins is normally carried out in a four-component system of water, a buffer, protein and precipitant, either salt or alcohol. With four components, at fixed pH, temperature and pressure, it is possible to vary the protein concentration and its solubility independently, because the solubility is determined by the precipitant concentration. This degree of freedom is useful in crystallizing rabbit muscle aldolase and lysozyme because the nucleation rate is a function only of the total protein concentration and not of the protein solubility. Large crystals are obtained when both the protein concentration and the protein solubility are small. The small protein concentration suppresses the rate of nucleation, and the small solubility provides sufficient protein to grow large crystals on the few nuclei. Sometimes it is desirable to grow crystals from seeds, especially if a special crystal form is required. In this case also, homogeneous nucleation of an unfavorable form may be avoided for aldolase through the use of low protein concentration.

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