An apparatus for electric-field-induced protein crystallization

Al‐Haq, Muhammad Imran; Lebrasseur, Éric; Choi, Wan-Kyu; Tsuchiya, H.; Torii, Tôru; Yamazaki, Hiroki; Shinohara, Etsuo

doi:10.1107/s0021889806049028

Cited by 33 publications

(37 citation statements)

References 6 publications

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“…It is also difficult to control the nucleation process of proteins, and therefore some research that has employed the application of electric fields to protein solutions [17,[33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48] has been actively performed. Almost all of this research used a DC electric field, and it was reported that the nucleation rate for protein crystals decreased.…”

Section: Introductionmentioning

confidence: 99%

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

et al. 2016

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X-ray diffraction (XRD) rocking-curves were measured for tetragonal hen egg white (HEW) lysozyme crystals grown with and without application of an external electric field, and the crystal quality was assessed according to the full width at half-maximums (FWHMs) of each rocking-curve profile. The average FWHMs for tetragonal HEW lysozyme crystals grown with an external electric field at 1 MHz were smaller than those for crystals grown without, especially for the 12 12 0 reflection. The crystal homogeneity of the tetragonal HEW lysozyme crystals was also improved under application of an external electric field at 1 MHz, compared to that without. Improvement of the crystal quality of tetragonal HEW lysozyme crystals grown under an applied field is discussed with a focus on subgrain formation. In addition, the origin of subgrain misorientation is also discussed with respect to the incorporation of impurities into protein crystals.

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Section: Introductionmentioning

confidence: 99%

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

et al. 2016

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“…A growth technique mediated by screw dislocations under low supersaturation has also been proposed [29][30][31][32]. Techniques in which an electric field is applied to a protein solution have also been actively investigated, with a focus on controlling the nucleation rate [33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48][49].…”

Section: Introductionmentioning

confidence: 99%

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

et al. 2017

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Dislocation-free tetragonal hen egg white (HEW) lysozyme crystals were grown from a seed crystal in a cell. The rates of tetragonal HEW lysozyme crystal growth normal to the (110) and (101) faces with and without a 1-MHz external electric field were measured. A decrease in the typical growth rates of the crystal measured under an applied field at 1 MHz was observed, although the overall driving force increased. Assuming that the birth and spread mechanism of two-dimensional nucleation occurs, an increase in the effective surface energy of the step ends was realized in the presence of the electric field, which led to an improvement in the crystal quality of the tetragonal HEW lysozyme crystals. This article also discusses the increase in the effective surface energy of the step ends with respect to the change in the entropy of the solid.

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“…While applying EFs, there occurs a reduction in the nucleation site numbers, accompanied by a rapid increase in lysozyme crystal size. A method for protein crystallization involving the use of a microbatch under oil (where the crystallizing protein is contained in a small droplet of solution dispensed on electrically isolated electrodes) and a relatively low voltage (30-270 V) has been developed by Al-Haq et al [46].…”

Section: Crystallization In the Presence Of Electric Fields (Efs)mentioning

confidence: 99%

Recent Insights into the Crystallization Process; Protein Crystal Nucleation and Growth Peculiarities; Processes in the Presence of Electric Fields

Nanev

2017

Crystals

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Three-dimensional protein molecule structures are essential for acquiring a deeper insight of the human genome, and for developing novel protein-based pharmaceuticals. X-ray diffraction studies of such structures require well-diffracting protein crystals. A set of external physical factors may promote and direct protein crystallization so that crystals obtained are useful for X-ray studies. Application of electric fields aids control over protein crystal size and diffraction quality. Protein crystal nucleation and growth in the presence of electric fields are reviewed. A notion of mesoscopic level of impact on the protein crystallization exercised by an electric field is also considered.Keywords: protein crystallization; classical and two-step nucleation mechanisms; impact of electric fields on the protein crystallization; external and internal electric fields; number density; size and quality of protein crystals

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An apparatus for electric-field-induced protein crystallization

Cited by 33 publications

References 6 publications

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

Technique for High-Quality Protein Crystal Growth by Control of Subgrain Formation under an External Electric Field

Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals

Recent Insights into the Crystallization Process; Protein Crystal Nucleation and Growth Peculiarities; Processes in the Presence of Electric Fields

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