Protein Crystal Growth Methods

Quezada, Andrea; Arreguı́n-Espinosa, Roberto; Moreno, Abel

doi:10.1007/978-3-540-74761-1_47

Cited by 6 publications

(5 citation statements)

References 142 publications

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“…The diffraction pattern, presented in figure S3, showed that the crystal was of protein and not of salt and they could be diffracted up to 6Å resolution. In fact, similar dendrite shape of ferritin crystal has been observed and analyzed by others as well 23 , who have attributed the dendritic growth of ferritin to oligomers of different chain length present in the protein solution. In our experiment, the crystal was constrained to grow within a confined space between the two parallel plates, which too appear to have influence on the crystal shape.…”

Section: Schematic Of Experimental Set-upsupporting

confidence: 77%

Disordered Nanowrinkle Substrates for Inducing Crystallization over a Wide Range of Concentration of Protein and Precipitant

Ghatak

2013

Langmuir

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There are large number of proteins, the existence of which are known but not their crystal structure, because of difficulty in finding the exact condition for their crystallization. Heterogeneous nucleation on disordered porous substrates with small yet large distribution of pores is considered a panacea for this problem, but a universal nucleant suitable for crystallizing large variety of proteins does not really exist. To this end, we report here a nanowrinkled substrate which displays remarkable ability and control over protein crystallization. Experiments with different proteins show that on these substrates crystals nucleate even at very low protein concentration in buffer. A small number of very large crystals appear for precipitant concentrations varied over orders of magnitude, ~0.003-0.3 M; for some proteins, crystals appear even without addition of any precipitant, not seen with any other heterogeneous substrates. In essence, these substrates significantly diminish the influence of the above two parameters, thought to be key factors for crystallization, signifying that this advantage can be exploited for finding out crystallization condition for other yet-to-be-crystallized proteins.

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Section: Schematic Of Experimental Set-upsupporting

confidence: 77%

Disordered Nanowrinkle Substrates for Inducing Crystallization over a Wide Range of Concentration of Protein and Precipitant

Ghatak

2013

Langmuir

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“…This theory indicates that the growth of the nucleus is a purely stochastic event, and that it is a competition between the increase in free energy, mainly due to an enthalpic factor of the forming nucleus's liquid-solid interphase surface, against the decrease in energy due to the formation of the solid. As illustrated in Figure 1, there is a critical radius, denoted as r', over which if the number of units of the nucleus being formed necessary to reach said radius is surpassed, the decrease in the free energy due to the formation of the solid allows the nucleus to remain thermodynamically stable and keep growing [21]. A more concise way of using this term could probably emerge from the effects of polymorphism itself.…”

Section: Nucleation and Polymorphismmentioning

confidence: 99%

“…Free energy of the nucleation[21]. With permit of the copyright (Copyright Clearance Center License 4635650204890).…”

mentioning

confidence: 99%

Crystal Growth in Gels from the Mechanisms of Crystal Growth to Control of Polymorphism: New Trends on Theoretical and Experimental Aspects

et al. 2019

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A gel can be considered to be a two-phase (liquid and solid) system, which lacks flow once it reaches a stationary state. The solid phase is usually a tridimensional polymeric mesh, while the liquid phase is usually found in three forms: contained in great cavities, retained in the capillary pores between micelles, or adsorbed on the surface of a micelle. The influence of the use of gels in crystal growth is diverse and depends on the type of gel being used. A decrease in solubility of any solute in the liquid may occur if the solvent interacts extensively with the polymeric section, hence, the nucleation in gels in these cases apparently occurs at relatively low supersaturations. However, if the pore size is small enough, there is a possibility that a higher supersaturation is needed, due to the compartmentalization of solvents. Finally, this may also represent an effect in the diffusion of substances. This review is divided into three main parts; the first evaluates the theory and practice used for the obtainment of polymorphs. The second part describes the use of gels into crystallogenesis of different substances. The last part is related to the particularities of protein crystal polymorphism, as well as modern trends in gel growth for high-resolution X-ray crystallography.

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“…Transport processes, and in particular mass transport, are very important for crystal growth from aqueous solutions. − Mass and heat transport processes are critical to the final quality and characteristics of the crystals . Many crystallogenesis techniques have been explicitly developed for controlling the relative contributions of convective and diffusive transport in crystal growth . During the active incorporation of ions or molecules in the three-dimensional lattice, density differences are generated in the proximal area of the developing faces leading to a convective flux in the surroundings of the crystal. − Convective transport of molecules competes with pure diffusive transport, and the sum of these two processes will determine the nature and the kinetics of nutrient presentation to the growing crystal.…”

Section: Introductionmentioning

confidence: 99%

Investigations into Protein Crystallization in the Presence of a Strong Magnetic Field

Surade

Ochi

Nietlispach

et al. 2009

Crystal Growth & Design

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A new strategy is proposed for batch crystallization of proteins in solution-growth or gel-growth by using the batch method inside capillary tubes applying magnetic fields. Four proteins with differing proportions of R-helices and β-sheets and crystallized in five different crystallographic space groups are studied, allowing an analysis of the anisotropy of the diamagnetic susceptibility of the peptide bond as well as the polarity of the space groups in the presence of a strong magnetic field of 11.75 T. The crystal quality is shown to be improved by using a strong magnetic field to orient protein molecules, and gel-growth (high concentrations of agar) to control the transport phenomena as well as crystal growth. Some advantages to increase the crystal quality for crystals from marginal conditions for X-ray diffraction, and disadvantages of the use of solution-and gel-growth (low concentration of agar) in magnetic fields, and their plausible applications to high resolution X-ray crystallography are discussed.

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Protein Crystal Growth Methods

Cited by 6 publications

References 142 publications

Disordered Nanowrinkle Substrates for Inducing Crystallization over a Wide Range of Concentration of Protein and Precipitant

Disordered Nanowrinkle Substrates for Inducing Crystallization over a Wide Range of Concentration of Protein and Precipitant

Crystal Growth in Gels from the Mechanisms of Crystal Growth to Control of Polymorphism: New Trends on Theoretical and Experimental Aspects

Investigations into Protein Crystallization in the Presence of a Strong Magnetic Field

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