Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen-egg-white lysozyme

Steinrauf, L. K.

doi:10.1107/s0365110x59000238

Cited by 171 publications

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“…As the temperature decreased, a few more water molecules became visible in the refined structure (see Table 2). The ordered water molecules consitute only about 1/4 of all crystalline water [assuming the lysozyme crystal as a 33.5% protein solution (Steinrauf, 1959)]. Much of the solvent remains disordered, even at very low temperature, and has an amorphous structure that cannot be modeled by an atomic model.…”

Section: Water Structure and Dynamicsmentioning

confidence: 99%

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The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

Kurinov¹,

Harrison²

1995

Acta Crystallogr D Biol Crystallogr

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Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 A, 3 from 295 to 250 K and about 220200 A 3 below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondarystructure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hingebending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.

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Section: Water Structure and Dynamicsmentioning

confidence: 99%

“…89F8276) was used without further purification. Tetragonal crystals were obtained, as reported previously (Steinrauf, 1959), using hanging-drop experiments with 0.1 M sodium acetate and 5% NaCI stock solution (pH =4.7) at room temperature. Lysozyme crystals about 0.8 mm in their largest dimension were used.…”

Section: Crystal Preparation and Data Collectionmentioning

confidence: 99%

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

Kurinov¹,

Harrison²

1995

Acta Crystallogr D Biol Crystallogr

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“…Monoclinic lysozyme nitrate has been grown from a 1% protein solution adjusted to pH 4.5 by addition of nitric acid, and 0.35 M sodium nitrate (Steinrauf, 1959). Although the temperature is not specified by the author, it is assumed to be room temperature.…”

Section: Introductionmentioning

confidence: 99%

“…Concerning the triclinic form of lysozyme nitrate, Steinrauf mentioned its preparation for the first time (Steinrauf, 1959), from a 1% protein solution with 0.23 M NaNO 3 in acetate buffer (25 mM sodium acetate and 25 mM acetic acid). The pH was finally adjusted to 4.5 by the addition of diluted nitric acid.…”

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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“…Thus, crystals of the tetragonal and monoclinic forms, grown under the usual conditions (Alderton, Ward & Fevold, 1945;Steinrauf, 1959), were kept in sealed thin-walled capillaries with a few drops of a saturated solution of potassium chromate (K2CrO4) for 15-20h. For both forms: (i) the protein molecules were found to be displaced from their positions in the native crystals along with the most strongly 'bound' water molecules and (ii) the most significant changes occurred in the inhibitor-binding region (Kodandapani, Cheravakkattumadhom & Vijayan, 1990;Madhusudan et al, 1993).…”

Section: Influence On Crystal Packingmentioning

confidence: 99%

Water structure associated with proteins and its role in crystallization

Frey¹

1994

Acta Cryst D

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X-ray or neutron diffraction studies have shown, at the atomic level, that water molecules occupy well determined sites inside or at the surface of biological macromolecules. These water molecules are constitutive of biomolecules and play a crucial role in their structural and functional properties. Upon crystallization some water molecules are either desolvated or involved in crystal packing. The role of water in determining crystal packing has been experimentally confirmed by several X-ray analyses.

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Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen-egg-white lysozyme

Cited by 171 publications

References 0 publications

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

Two polymorphs of lysozyme nitrate: temperature dependence of their solubility

Water structure associated with proteins and its role in crystallization

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