Growth kinetics of protein single crystals in the gel acupuncture technique

García‐Ruiz, Juan Manuel; Moreno, Abel

doi:10.1016/s0022-0248(96)01188-8

Cited by 28 publications

(18 citation statements)

References 23 publications

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“…In the first part, we will outline, how impurities affect the growth and in the second part, we will demonstrate the selfpurification process, which takes place under diffusive (microgravity-like) transport conditions due to the extension of the depletion zone. This process was postulated by numerical simulations for ferritin [38] and lysozyme [39] and was corroborated by measurements of segregation coefficients for convective and diffusive transport conditions [40] and by analyzing the concentration field around growing crystals under microgravity [41] and in gelled solutions [42][43][44]. This self-purification mechanism is verified by our in situ observation of the growth process.…”

Section: Introductionsupporting

confidence: 73%

Step velocity in tetragonal lysozyme growth as a function of impurity concentration and mass transport conditions

Dold

Ono

Tsukamoto

et al. 2006

Journal of Crystal Growth

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Section: Introductionsupporting

confidence: 73%

Step velocity in tetragonal lysozyme growth as a function of impurity concentration and mass transport conditions

Dold

Ono

Tsukamoto

et al. 2006

Journal of Crystal Growth

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“…It was found with two proteins that the maximum value of the growth rate, recorded at the early stages of growth before solution depletion and transport control set in, is 1.5-3 times lower than the equivalent value in free solutions (43). This suggests that the kinetic coefficient of growth is correlated to the diffusivity.…”

Section: Resultsmentioning

confidence: 95%

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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“…Specific ''noncrystallographic'' shapes of shells and other fossils have served for a long time as an evidence of life on earth. However, it was shown recently [4,5] that these weird shapes may be obtained in the laboratory in purely inorganic systems with calcium silicates. Biomineralization has been studied for decades, but quantitative understanding on a molecular level is still missing.…”

Section: Biologymentioning

confidence: 99%