Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations

Fredericks, William J.; Hammonds, M.C.; Howard, Sandra B.; Rosenberger, Franz

doi:10.1016/0022-0248(94)90111-2

Cited by 83 publications

(55 citation statements)

References 22 publications

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“…Hence, the narrow range of the activation barriers is unexpected for transitionstate kinetics, where the activated complexes should ref lect the chemical variety of the crystallizing compounds. On the other hand, assuming diffusion-limited kinetics, we note that the diffusivities in aqueous solutions have effective activation energies of Ϸ8 -17 kJ⅐mol Ϫ1 (21,34). If, as suggested by Eq.…”

Section: Resultsmentioning

confidence: 99%

“…n 0 ϭ 1.3320 is the refractive index of the solvent at the wavelength of the laser beam ϭ 0.6328 m (21,22), dn͞dC is the n increment with the protein concentration, C, determined for each protein at ϭ 0.628 m by a differential refractometer (Wyatt Technology, Santa Barbara, CA). For ferritin dn͞dC ϭ 0.290 cm 3 ⅐g Ϫ1 ; for apoferritin, dn͞dC ϭ 0.159 cm 3 ⅐g Ϫ1 .…”

Section: Characterization Of the Molecular Masses And Pair Interactiomentioning

confidence: 99%

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Diffusion-limited kinetics of the solution–solid phase transition of molecular substances

Petsev

Chen

Gliko

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

105

131

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For critical tests of whether diffusion-limited kinetics is an option for the solution-solid phase transition of molecular substances or whether they are determined exclusively by a transition state, we performed crystallization experiments with ferritin and apoferritin, a unique pair of proteins with identical shells but different molecular masses. We find that the kinetic coefficient for crystallization is identical (accuracy <7%) for the pair, indicating diffusion-limited kinetics of crystallization. Data on the kinetics of this phase transition in systems ranging from small-molecule ionic to protein and viri suggest that the kinetics of solution-phase transitions for broad classes of small-molecule and protein materials are diffusion-limited.T he kinetics of the reactions in solutions are either limited only by the rate of diffusion of the species (1) or additionally slowed down by a transition state (2). For the kinetics of the phase transitions in solutions, it is generally accepted that colloid particles follow the diffusion-limited model, whereas the growth rates of new phases of small molecules are thought to be governed by a transition state (3-7). For the intermediate case of protein solid phases, the growth kinetics largely resemble those of small molecules, and it was assumed that transition-state laws apply (8). Although rate laws reminiscent of diffusionlimited mechanisms have been postulated for small-molecule phase transitions (9-11), they were viewed as equivalent to respective transition-state expressions (10, 11), and no critical tests to discriminate between the two mechanisms were suggested or performed.In the transition-state kinetics, the rate coefficients are (i) mass-dependent (12, 13), (ii) independent on the diffusivity (2), and (iii) faster for high-symmetry molecules because of the transition-state entropy (7). Hence, for tests of the mechanism of growth of the new phase during a solution-solid phase transition, we selected the crystallization of ferritin͞ apoferritin, a unique pair of proteins that share a nearspherical protein shell, consisting of 24 identical subunits (14, 15). The crystals of ferritin and apoferritin are typically faceted by octahedral [111] faces and have been shown to grow by the lateral spreading of layers generated by two-dimensional nucleation (16, 17). For apoferritin, it was shown that the edges of the unfinished layers, called growth steps, propagate by the incorporation of single protein molecules at the growth sites, kinks (16,18). In the face-centered cubic lattice that ferritin and apoferritin share, kinks are defined as the termination points of three independent ͗011͘ rows of molecules belonging to the unfinished layer (19). Thus, the step velocity equals the product of the molecular diameter a, mean kink density n k Ϫ1 , and net molecular f lux into a kink (j ϩ Ϫ j Ϫ ) (16, 18). Methods Characterization of the Molecular Masses and Pair Interactions ofFerritin and Apoferritin. We performed static light scattering (20) in 0.2 M NaOOCCH 3 solutions....

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Section: Resultsmentioning

confidence: 99%

Section: Characterization Of the Molecular Masses And Pair Interactiomentioning

confidence: 99%

Diffusion-limited kinetics of the solution–solid phase transition of molecular substances

Petsev

Chen

Gliko

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

105

131

View full text Add to dashboard Cite

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“…21 The stress on the growth cell resulting from the thermal expansion of the growth solution, σ q , can be calculated with Hooke's law as follows:…”

Section: A Cell Bodymentioning

confidence: 99%

Development of compartment for studies on the growth of protein crystals in space

Yamazaki

Tsukamoto

Yoshizaki

et al. 2016

Review of Scientific Instruments

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Articles you may be interested inModeling crystal growth from solution with molecular dynamics simulations: Approaches to transition rate constants J. Chem. Phys. 136, 034704 (2012) To clarify the growth mechanism of a protein crystal, it is essential to measure its growth rate with respect to the supersaturation. We developed a compartment (growth cell) for measuring the growth rate (<0.1 nm s −1 ) of the face of a protein crystal at a controlled supersaturation by interferometry over a period of half a year in space. The growth cell mainly consists of quartz glass, in which the growth solution and a seed crystal are enclosed by capillaries, the screw sample holder, and a helical insert. To avoid the destruction of the cell and the evaporation of the water from the solution inside the cell, we selected the materials for these components with care. The equipment was successfully used to examine the growth of a lysozyme crystal at a controlled supersaturation in space, where convection is negligible because of the microgravity environment, thereby advancing our understanding of the mechanism of protein crystal growth from solution. The technique used to develop the growth cell is useful not only for space experiments but also for kinetic studies of materials with very slow growth and dissolution rates (<10 −3 nm s −1 ). C 2016 AIP Publishing LLC. [http://dx

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“…Aufgrund ihrer Gröûe eignen sich Proteine hervorragend für Lichtstreuexperimente. Mittels quasi-elastischer Lichtstreuung haben Fredericks et al [30] sowie Rosenberger et al [31] den Nachweis der Präaggregation von Proteinmolekülen in Lösung geführt. Bernardo et al [32] untersuchten die Übersättigungs-und pH-Abhängigkeit der Induktionszeit bei der Keimbildung von Schweineinsulin und HEWL unter Verwendung der UV-Absorption.…”

Section: Kinetik Der Proteinkristallisationunclassified

Industrielle Kristallisation von Proteinen - Eine Frage der Aktivität

Jones

Ulrich

2005

Chemie Ingenieur Technik

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Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations

Cited by 83 publications

References 22 publications

Diffusion-limited kinetics of the solution–solid phase transition of molecular substances

Diffusion-limited kinetics of the solution–solid phase transition of molecular substances

Development of compartment for studies on the growth of protein crystals in space

Industrielle Kristallisation von Proteinen - Eine Frage der Aktivität

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