Special Issue "Protein Crystallization under the Presence of an Electric Field"

A special issue of Crystals (ISSN 2073-4352). This special issue belongs to the section "Biomolecular Crystals".

Deadline for manuscript submissions: closed (30 September 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Abel Moreno

Instituto de Química, Universidad Nacional Autonoma de Mexico, Mexico City, 04510, Mexico
Website | E-Mail
Interests: Protein Crystallogenesis, Crystal Growth, Crystallochemistry, Biomineralization Processes

Special Issue Information

Dear Colleagues,

Nowadays, the use of electrically-assisted protein crystallization methods by using direct current (DC) or alternating current (AC), has revealed that, on average, crystals grow better in crystal quality and oriented to the cathode (when the protein molecule was positively charged), compared to the crystals grown on the anode (which is a negatively charged protein molecule). These electro-assisted crystallization techniques also enable the growth of protein crystals, as a function of temperature, under the influence of DC or AC electric fields. It has also permitted the isolation of protein polymorphs, as published elsewhere. According to recent publications, AC current could affect not only the number of crystals, but also their size, depending on its frequency. Up to now, the trend in crystal growth for protein models studied is as follows: The higher the AC the higher the number of crystals; in the near future this can be applicable to the free electron lasers (XFEL) experiments for solving complicated protein structures using the fourth generation of synchrotrons all over the world. There have been a significant number of publications focused on this topic recently, which is why the thematic issue in “Protein Crystallization under the Presence of an Electric Field” for the Crystals journal (ISSN 2073-4352, http://www.mdpi.com/journal/crystals) will be published soon. We encourage all specialists and experts on this topic to submit original contributions to this journal, and to the thematic issue for consideration and publication.

Prof. Dr. Abel Moreno
Guest Editor

Manuscript Submission Information

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Keywords

•    Electric Fields
•    Protein Electrocrystallization
•    Electrochemically-assisted Protein Crystallization
•    Crystal Growth under the Presence of Electric Currents (DC/AC)

Published Papers (5 papers)

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Research

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Open AccessArticle Crystallization under an External Electric Field: A Case Study of Glucose Isomerase
Crystals 2017, 7(7), 206; doi:10.3390/cryst7070206
Received: 9 May 2017 / Revised: 8 June 2017 / Accepted: 9 June 2017 / Published: 6 July 2017
Cited by 2 | PDF Full-text (3179 KB) | HTML Full-text | XML Full-text
Abstract
Electric fields have been employed to promote macromolecular crystallization for several decades. Although crystals grown in electric fields seem to present higher diffraction quality, these methods are not widespread. For most configurations, electrodes are in direct contact with the protein solution. Here, we
[...] Read more.
Electric fields have been employed to promote macromolecular crystallization for several decades. Although crystals grown in electric fields seem to present higher diffraction quality, these methods are not widespread. For most configurations, electrodes are in direct contact with the protein solution. Here, we propose a configuration that can be easily extended to standard crystallization methods for which the electrodes are not in direct contact with the protein solution. Furthermore, the proposed electrode configuration supplies an external DC electric field. Glucose Isomerase from Streptomyces rubiginosus crystals were grown at room temperature using the microbatch method in the presence of 1, 2, 4, and 6 kV. Several crystallization trials were carried out for reproducibility and statistical analysis purposes. The comparison with crystals grown in the absence of electric fields showed that crystallization in the presence of electric fields increases the size of crystals, while decreasing the number of nucleations. X-ray diffraction analysis of the crystals showed that those grown in the presence of electric fields are of higher crystal quality. Full article
(This article belongs to the Special Issue Protein Crystallization under the Presence of an Electric Field)
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Open AccessArticle Electro-Infiltration of Cytochrome C into a Porous Silicon Network, and Its Effect on Nucleation and Protein Crystallization—Studies of the Electrical Properties of Porous Silicon Layer-Protein Systems for Applications in Electron-Transfer Biomolecular Devices
Crystals 2017, 7(7), 194; doi:10.3390/cryst7070194
Received: 6 May 2017 / Revised: 10 June 2017 / Accepted: 23 June 2017 / Published: 28 June 2017
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Abstract
In this work, we report the electrical properties of cytochrome C (Cyt C) inside porous silicon (PSi). We first used two techniques of protein infiltration: classic sitting drop and electrochemical migration methods. The electrochemically assisted cell, used for the infiltration by electro-migration, improved
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In this work, we report the electrical properties of cytochrome C (Cyt C) inside porous silicon (PSi). We first used two techniques of protein infiltration: classic sitting drop and electrochemical migration methods. The electrochemically assisted cell, used for the infiltration by electro-migration, improved the Cyt C nucleation and the crystallization behavior due to the PSi. We were able to carry out the crystallization thanks to the previous infiltration of proteins inside the Si pores network. We then continued the protein crystal growth through a vapor diffusion set-up. Secondly, we applied both forward and reverse bias currents only to the infiltrated Cyt C. Finally, the electrical characteristics were compared to the control (the protein molecules of which were not infiltrated) and to the samples without protein infiltration. The linker used in the sitting drop method influenced the electrical properties, which showed a modification in the current density. The simple drop method showed a current density of ~42 A/cm2; when employing the electrochemical cell technique, the current density was ~318 A/cm2; for the crystallized structures, it was ~0.908 A/cm2. Full article
(This article belongs to the Special Issue Protein Crystallization under the Presence of an Electric Field)
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Open AccessArticle Crystal Growth of High-Quality Protein Crystals under the Presence of an Alternant Electric Field in Pulse-Wave Mode, and a Strong Magnetic Field with Radio Frequency Pulses Characterized by X-ray Diffraction
Crystals 2017, 7(6), 179; doi:10.3390/cryst7060179
Received: 29 April 2017 / Revised: 12 June 2017 / Accepted: 15 June 2017 / Published: 19 June 2017
Cited by 1 | PDF Full-text (3177 KB) | HTML Full-text | XML Full-text
Abstract
The first part of this research was devoted to investigating the effect of alternate current (AC) using four different types of wave modes (pulse-wave) at 2 Hz on the crystal growth of lysozyme in solution. The best results, in terms of size and
[...] Read more.
The first part of this research was devoted to investigating the effect of alternate current (AC) using four different types of wave modes (pulse-wave) at 2 Hz on the crystal growth of lysozyme in solution. The best results, in terms of size and crystal quality, were obtained when protein crystals were grown under the influence of electric fields in a very specific wave mode (“breathing” wave), giving the highest resolution up to 1.34 Å in X-ray diffraction analysis compared with controls and with those crystals grown in gel. In the second part, we evaluated the effect of a strong magnetic field of 16.5 Tesla combined with radiofrequency pulses of 0.43 μs on the crystal growth in gels of tetragonal hen egg white (HEW) lysozyme. The lysozyme crystals grown, both in solution applying breathing-wave and in gel under the influence of this strong magnetic field with pulses of radio frequencies, produced the larger-in-size crystals and the highest resolution structures. Data processing and refinement statistics are very good in terms of the resolution, mosaicity and Wilson B factor obtained for each crystal. Besides, electron density maps show well-defined and distinctly separated atoms at several selected tryptophan residues for the crystal grown using the “breathing wave pulses”. Full article
(This article belongs to the Special Issue Protein Crystallization under the Presence of an Electric Field)
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Open AccessArticle Effect of an External Electric Field on the Kinetics of Dislocation-Free Growth of Tetragonal Hen Egg White Lysozyme Crystals
Crystals 2017, 7(6), 170; doi:10.3390/cryst7060170
Received: 28 April 2017 / Revised: 30 May 2017 / Accepted: 9 June 2017 / Published: 10 June 2017
Cited by 2 | PDF Full-text (768 KB) | HTML Full-text | XML Full-text
Abstract
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
[...] Read more.
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. Full article
(This article belongs to the Special Issue Protein Crystallization under the Presence of an Electric Field)
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Review

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Open AccessReview Recent Insights into the Crystallization Process; Protein Crystal Nucleation and Growth Peculiarities; Processes in the Presence of Electric Fields
Crystals 2017, 7(10), 310; doi:10.3390/cryst7100310
Received: 22 September 2017 / Revised: 11 October 2017 / Accepted: 12 October 2017 / Published: 15 October 2017
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Abstract
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
[...] Read more.
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. Full article
(This article belongs to the Special Issue Protein Crystallization under the Presence of an Electric Field)
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