Crystallization in Gels

Moreno, Abel; Mendoza, M.E.

doi:10.1016/b978-0-444-63303-3.00031-6

Cited by 12 publications

(12 citation statements)

References 209 publications

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Section: Resultsmentioning

confidence: 99%

“…The most important part for this obtainment of high-quality single crystals is the growth under diffusion-control transport in gels. These gel-growth methods have been recently reviewed [119][120][121]. We can obtain two main advantages when applying this methodology for growing crystals; the first is as follows: when applying this all-inclusive method, the higher the content of alpha helices in We can obtain two main advantages when applying this methodology for growing crystals; the first is as follows: when applying this all-inclusive method, the higher the content of alpha helices in the protein is, the higher the crystal improvement in terms of crystal quality will be.…”

Section: Resultsmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

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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“…This agreed beneficial effect of the diffusive mass-transport regime on crystal quality, together with the economic costs associated with experiments in space, were the driving force when considering further existing ground-based alternatives to mimic this specific mass-transport scenario [23]. Several approaches have been proposed to eliminate/reduce gravity-induced convection on Earth [24][25][26][27][28][29][30], but one of the most commonly used techniques, due to its ease of implementation, is that of gelling the growth media [31][32][33]. Agarose, a thermo-reversible hydrophilic hydrogel, is the most commonly used gelling additive due to its frequent use in bio-laboratories and its ease of preparation.…”

Section: Introductionmentioning

confidence: 99%

On the Quality of Protein Crystals Grown under Diffusion Mass-transport Controlled Regime (I)

et al. 2020

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It has been previously shown that the diffraction quality of protein crystals strongly depends on mass transport during their growth. In fact, several studies support the idea that the higher the contribution of the diffusion during mass transport, the better the diffraction quality of the crystals. In this work, we have compared the crystal quality of two model (thaumatin and insulin) and two target (HBII and HBII-III) proteins grown by two different methods to reduce/eliminate convective mass transport: crystal growth in agarose gels and crystal growth in solution under microgravity. In both cases, we used identical counterdiffusion crystallization setups and the same data collection protocols. Additionally, critical parameters such as reactor geometry, stock batches of proteins and other chemicals, temperature, and duration of the experiments were carefully monitored. The diffraction datasets have been analyzed using a principal component analysis (PCA) to determine possible trends in quality indicators. The relevant indicators show that, for the purpose of structural crystallography, there are no obvious differences between crystals grown under reduced convective flow in space and convection-free conditions in agarose gel, indicating that the key factor contributing to crystal quality is the reduced convection environment and not how this reduced convection is achieved. This means that the possible detrimental effect on crystal quality due to the incorporation of gel fibers into the protein crystals is insignificant compared to the positive impact of an optimal convection-free environment provided by gels. Moreover, our results confirm that the counterdiffusion technique optimizes protein crystal quality and validates both environments in order to deliver high quality protein crystals, although other considerations, such as protein/gel interactions, must be considered when defining the optimal crystallization setup.

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“…In the biological macromolecules field, where sample impurity has been a relevant issue for many years, it is generally thought that the participation of any new additive, such as gel precursors, could be detrimental to the crystallization, affecting the final crystal properties. In contrast, it is well accepted that the use of gels may help control and facilitate the growth of bigger and higher-quality crystals for inorganic materials [1][2][3]. Nowadays, researchers are being convinced about the advantages of using gels in protein crystallization, such as the reduction of sedimentation, the inhibition of twinning formation, and the reduction of convective flow, which simulates microgravity conditions [4].…”

Section: Introductionmentioning

confidence: 99%

“…Generally, agarose gels [4] are the most used gel for protein crystallization due to their easy preparation and handling. Other gels such as silica, polyethylene oxide (PEO), polyacrylamide, dextran, sephadex, cellulose gels, or their derivatives, including methyl or hydroxymethyl derivatives, have also been tested in biomacromolecules' crystallization [3,4]. More recently, novel gels based on polymers such as polyvinyl alcohol, calcium alginate beads, or new synthetic ones such as poly(N-isopropyl-acrylamide-co-n-butyl methacrylate) [3] and hydrophilic PEG (poly(ethylene glycol)) [11] have also been tested in protein crystallization.…”

Section: Introductionmentioning

confidence: 99%

Extending the pool of compatible peptide hydrogels for protein crystallization

et al. 2019

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Short-peptide supramolecular (SPS) hydrogels are a class of materials that have been found to be useful for (bio)technological applications thanks to their biocompatible nature. Among the advantages reported for these peptides, their economic affordability and easy functionalization or modulation have turned them into excellent candidates for the development of functional biomaterials. We have recently demonstrated that SPS hydrogels can be used to produce high-quality protein crystals, improve their properties, or incorporate relevant materials within the crystals. In this work, we prove that hydrogels based on methionine and tyrosine are also good candidates for growing high-quality crystals of the three model proteins: lysozyme, glucose isomerase, and thaumatin.

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Crystallization in Gels

Cited by 12 publications

References 209 publications

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

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

On the Quality of Protein Crystals Grown under Diffusion Mass-transport Controlled Regime (I)

Extending the pool of compatible peptide hydrogels for protein crystallization

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