Special Issue "Novel Strategies for Improved Protein Crystallization"

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

Deadline for manuscript submissions: 15 December 2020.

Special Issue Editors

Dr. Ana Luísa Carvalho
Website
Guest Editor
UCIBIO, Faculdade de Ciências e Tecnologia, NOVA University of Lisbon, Department of Chemistry, 2829-516 Caparica, Portugal
Interests: structural biology; protein crystallization; macromolecular interactions; integrative methods; science outreach
Prof. Dr. Maria João Romão
Website
Guest Editor
UCIBIO, Faculdade de Ciências e Tecnologia, NOVA University of Lisbon, Department of Chemistry, 2829-516 Caparica, Portugal
Interests: structural biology; protein crystallization; metalloenzymes and enzymatic mechanisms; molybdoenzymes; science outreach and teaching

Special Issue Information

Dear Colleagues,

Although new structural biology approaches are arising, X-ray crystallography is still the most powerful and common method for gaining detail on the 3D structure of proteins. However, its success relies strongly on the availability of suitable crystals. Macromolecular crystallization is a critical step and the major bottleneck in solving a structure, since no generalized method exists that allows one to obtain the best conditions to crystallize a protein of interest. Therefore, important biological structures and details on their active sites remain unsolved due to the lack of suitable crystals, and there is an urgent need for more general and rational crystallization methods.

This is the motivation for this Special Issue on "Novel Strategies for Improved Protein Crystallization", which will tackle the problem by gathering current knowledge on novel approaches to improve the rate-determining nucleation step and/or to optimize existing crystallization conditions.

In the search for more universal crystallization tools, in particular nucleation-based techniques applicable to soluble and membrane proteins, recent methodologies include, for example, functionalized nano- and microparticles, tailored ionic liquids, and controlled crystallization devices. These methods intend to promote nucleation and crystal growth of difficult-to-crystallize macromolecules, and studies generally involve model proteins, to test and validate the new approaches.

This Special Issue is an opportunity to gather the expertise from chemists, biochemical engineers, biotechnologists, and crystallographers that will present strategies to tackle the crystallization problems of biological macromolecules. This Issue is expected to have a broad impact not only in academia but also in the pharmaceutic and biotechnological industries, which are continuously searching for reliable and robust methods that will speed up the crystal structure determination of valuable protein targets.

Candidate manuscripts are welcome reporting advances in the crystallisation of macromolecules not only limited to tradicional X-ray crystallography methods. Protein crystallization is also a challenge in the production of nano-sized crystals for Serial Femtosecond Crystallography (SFX) or large-sized crystals for Neutron Diffraction.

Dr. Ana Luísa Carvalho
Prof. Dr. Maria João Romão
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Crystals is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • protein crystallization methods
  • triggers of crystal nucleation
  • functional materials for protein stabilization and nucleation
  • protein crystal growth
  • nanoparticles in crystallization
  • ionic liquids in crystallization
  • devices for crystallization
  • automated crystallization
  • protein crystal stabilization and manipulation

Published Papers (4 papers)

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Research

Open AccessArticle
Enhancing Protein Crystallization under a Magnetic Field
Crystals 2020, 10(9), 821; https://doi.org/10.3390/cryst10090821 - 16 Sep 2020
Abstract
High-quality crystals are essential to ensure high-resolution structural information. Protein crystals are controlled by many factors, such as pH, temperature, and the ion concentration of crystalline solutions. We previously reported the development of a device dedicated to protein crystallization. In the current study, [...] Read more.
High-quality crystals are essential to ensure high-resolution structural information. Protein crystals are controlled by many factors, such as pH, temperature, and the ion concentration of crystalline solutions. We previously reported the development of a device dedicated to protein crystallization. In the current study, we have further modified and improved our device. Exposure to external magnetic field leads to alignment of the crystal toward a preferred direction depending on the magnetization energy. Each material has different magnetic susceptibilities depending on the individual direction of their unit crystal cells. One of the strategies to acquire a large crystal entails controlling the nucleation rate. Furthermore, exposure of a crystal to a magnetic field may lead to new morphologies by affecting the crystal volume, shape, and quality. Full article
(This article belongs to the Special Issue Novel Strategies for Improved Protein Crystallization)
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Open AccessArticle
Tools to Ease the Choice and Design of Protein Crystallisation Experiments
Crystals 2020, 10(2), 95; https://doi.org/10.3390/cryst10020095 - 07 Feb 2020
Cited by 1
Abstract
The process of macromolecular crystallisation almost always begins by setting up crystallisation trials using commercial or other premade screens, followed by cycles of optimisation where the crystallisation cocktails are focused towards a particular small region of chemical space. The screening process is relatively [...] Read more.
The process of macromolecular crystallisation almost always begins by setting up crystallisation trials using commercial or other premade screens, followed by cycles of optimisation where the crystallisation cocktails are focused towards a particular small region of chemical space. The screening process is relatively straightforward, but still requires an understanding of the plethora of commercially available screens. Optimisation is complicated by requiring both the design and preparation of the appropriate secondary screens. Software has been developed in the C3 lab to aid the process of choosing initial screens, to analyse the results of the initial trials, and to design and describe how to prepare optimisation screens. Full article
(This article belongs to the Special Issue Novel Strategies for Improved Protein Crystallization)
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Open AccessArticle
Monitoring the Production of High Diffraction-Quality Crystals of Two Enzymes in Real Time Using In Situ Dynamic Light Scattering
Crystals 2020, 10(2), 65; https://doi.org/10.3390/cryst10020065 - 23 Jan 2020
Abstract
The reproducible preparation of well-diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter [...] Read more.
The reproducible preparation of well-diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter the composition of the mother liquor during the experiment. We have applied this technology to study the crystallization of two enzymes, the CCA-adding enzyme of the psychrophilic bacterium Planococcus halocryophilus, and the lysozyme from hen egg white in the presence of a synthetic chemical nucleant. We were able to (i) detect early nucleation events and (ii) drive the crystallization system (through cycles of dissolution/crystallization) toward growth conditions yielding crystals with excellent diffraction properties. This technology opens a way to the rational production of samples for crystallography, ranging from nanocrystals for electron diffraction, microcrystals for serial or conventional X-ray diffraction, to larger crystals for neutron diffraction. Full article
(This article belongs to the Special Issue Novel Strategies for Improved Protein Crystallization)
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Open AccessFeature PaperArticle
Analysis of Glulisine Crystallisation Utilising Phase Diagrams and Nucleants
Crystals 2019, 9(9), 462; https://doi.org/10.3390/cryst9090462 - 03 Sep 2019
Abstract
Glulisine is a US Food and Drug Administration (FDA) approved insulin analogue, used for controlling hyperglycaemia in patients with diabetes mellitus (DM). It is fast acting which better approximates physiological insulin secretion, improving patient outcome. Crystallisation of Glulisine was analysed by its crystallisation [...] Read more.
Glulisine is a US Food and Drug Administration (FDA) approved insulin analogue, used for controlling hyperglycaemia in patients with diabetes mellitus (DM). It is fast acting which better approximates physiological insulin secretion, improving patient outcome. Crystallisation of Glulisine was analysed by its crystallisation phase diagram and nucleation-inducing materials. Both the hanging drop vapour diffusion and microbatch-under-oil methods were used and compared. We have shown that the same protein can have different solubility behaviours depending on the nature of the salt in the precipitating agent. In the case of Glulisine with magnesium formate, lowering the precipitant concentration drove the system further into supersaturation resulting in the formation of crystals and precipitation. This was the opposite effect to the usual scenario where raising the precipitant concentration leads to supersaturation. Glulisine with sodium potassium tartrate tetrahydrate (NaKT) followed the expected trend of forming crystals or precipitate at higher concentrations and clear drops at lower concentrations of the precipitant. The outcomes of crystallisation using the different crystallisation methods is also described. Glulisine was successfully crystallised and the crystals diffracted up to a resolution limit of 1.4 Å. Full article
(This article belongs to the Special Issue Novel Strategies for Improved Protein Crystallization)
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