Biological and Biogenic Crystallization

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

Deadline for manuscript submissions: closed (31 July 2017) | Viewed by 48537

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Special Issue Editor

Institute of Physics, Lodz University of Technology, ul. Wólczańska 219, 93-005 Łódź, Poland
Interests: biogenic crystals; crystal growth from solutions; crystal morphology; struvite; carbonate apatite; infectious urinary stones
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Dear Colleagues,

The first biological crystals were grown in the beginning of the 20th century. The first diffraction pattern of biological crystal was done for the enzyme pepsin, which, at the same time, was one of the first enzymes to be crystallized. Soon after that, the tobacco mosaic virus was crystallized. Since that time biological crystals have become the subjects of intensive research work.

Biogenic crystals are produced by living organisms, they include  for example, calcium oxalate crystals produced in different plant tissues or magnetite crystals forming inside different bacteria and animals or various crystals in human body appearing  in the course of physiological and pathological processes. Biogenic crystals attract a lot of attention because of their fascinating and unique properties.

The theme of this Special Issue is "Biological and Biogenic Crystallization". Our intention is to create international platform aimed at covering a broad description of results involving crystallization of biological molecules including virus and protein crystallization, biogenic crystallization including physiological and pathological crystallization taking place in living organisms (human beings, animals, plants, bacteria, etc.) and bio-inspired crystallization. Scientists working in a wide range of disciplines are welcome to present their recent research and development activities in all mentioned aspects of biological and biogenic crystallization.

Prof. Dr. Jolanta Prywer
Guest Editor

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Keywords

  • biological crystals

  • biogenic crystals

  • bio-inspired crystallization

Published Papers (7 papers)

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Research

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15 pages, 4225 KiB  
Article
In Situ Random Microseeding and Streak Seeding Used for Growth of Crystals of Cold-Adapted β-d-Galactosidases: Crystal Structure of βDG from Arthrobacter sp. 32cB
by Maria Rutkiewicz-Krotewicz, Agnieszka J. Pietrzyk-Brzezinska, Marta Wanarska, Hubert Cieslinski and Anna Bujacz
Crystals 2018, 8(1), 13; https://doi.org/10.3390/cryst8010013 - 01 Jan 2018
Cited by 5 | Viewed by 6321
Abstract
There is an increasing demand for cold-adapted enzymes in a wide range of industrial branches. Nevertheless, structural information about them is still scarce. The knowledge of crystal structures is important to understand their mode of action and to design genetically engineered enzymes with [...] Read more.
There is an increasing demand for cold-adapted enzymes in a wide range of industrial branches. Nevertheless, structural information about them is still scarce. The knowledge of crystal structures is important to understand their mode of action and to design genetically engineered enzymes with enhanced activity. The most difficult task and the limiting step in structural studies of cold-adapted enzymes is their crystallization, which should provide well-diffracting monocrystals. Herein, we present a combination of well-established crystallization methods with new protocols based on crystal seeding that allowed us to obtain well-diffracting crystals of two cold-adapted β-d-galactosidases (βDGs) from Paracoccus sp. 32d (ParβDG) and from Arthrobacter sp. 32cB (ArthβDG). Structural studies of both βDGs are important for designing efficient and inexpensive enzymatic tools for lactose removal and synthesis of galacto-oligosaccharides (GOS) and hetero-oligosaccharides (HOS), food additives proved to have a beneficial effect on the human immune system and intestinal flora. We also present the first crystal structure of ArthβDG (PDB ID: 6ETZ) determined at 1.9 Å resolution, and compare it to the ParβDG structure (PDB ID: 5EUV). In contrast to tetrameric lacZ βDG and hexameric βDG from Arthrobacter C2-2, both of these βDGs are dimers, unusual for the GH2 family. Additionally, we discuss the various crystallization seeding protocols, which allowed us to obtain ParβDG and ArthβDG monocrystals suitable for diffraction experiments. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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12461 KiB  
Article
Formation Mechanism of CaCO3 Spherulites in the Myostracum Layer of Limpet Shells
by Shitao Wu, Chang-Yang Chiang and Wuzong Zhou
Crystals 2017, 7(10), 319; https://doi.org/10.3390/cryst7100319 - 23 Oct 2017
Cited by 19 | Viewed by 7526
Abstract
CaCO3 spherulites were found in the myostracum layer of common limpet shells collected from East Sands, St Andrews, Scotland. Their microstructures were revealed by using powder X-ray diffraction, scanning electron microscopy, high-resolution transmission electron microscopy, and energy dispersive X-ray microanalysis. The formation [...] Read more.
CaCO3 spherulites were found in the myostracum layer of common limpet shells collected from East Sands, St Andrews, Scotland. Their microstructures were revealed by using powder X-ray diffraction, scanning electron microscopy, high-resolution transmission electron microscopy, and energy dispersive X-ray microanalysis. The formation mechanisms of these spherulites and their morphology evolution were postulated. It was proposed that spherical particles of an inorganic and biological composite formed first. In the centre of each spherical particle a double-layer disk of vaterite crystal sandwiching a biological sheet developed. The disk crystal supplies a relatively strong mirror symmetric dipole field, guiding the orientations of the nanocrystallites and the arrangement of mesorods and, therefore, determining the final morphology of the spherulite. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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1391 KiB  
Article
Modulating Nucleation by Kosmotropes and Chaotropes: Testing the Waters
by Ashit Rao, Denis Gebauer and Helmut Cölfen
Crystals 2017, 7(10), 302; https://doi.org/10.3390/cryst7100302 - 06 Oct 2017
Cited by 5 | Viewed by 6232
Abstract
Water is a fundamental solvent sustaining life, key to the conformations and equilibria associated with solute species. Emerging studies on nucleation and crystallization phenomena reveal that the dynamics of hydration associated with mineral precursors are critical in determining material formation and growth. With [...] Read more.
Water is a fundamental solvent sustaining life, key to the conformations and equilibria associated with solute species. Emerging studies on nucleation and crystallization phenomena reveal that the dynamics of hydration associated with mineral precursors are critical in determining material formation and growth. With certain small molecules affecting the hydration and conformational stability of co-solutes, this study systematically explores the effects of these chaotropes and kosmotropes as well as certain sugar enantiomers on the early stages of calcium carbonate formation. These small molecules appear to modulate mineral nucleation in a class-dependent manner. The observed effects are finite in comparison to the established, strong interactions between charged polymers and intermediate mineral forms. Thus, perturbations to hydration dynamics of ion clusters by co-solute species can affect nucleation phenomena in a discernable manner. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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1415 KiB  
Communication
Over-Production, Crystallization, and Preliminary X-ray Crystallographic Analysis of a Coiled-Coil Region in Human Pericentrin
by Min Ye Kim, Jeong Kuk Park, Yeowon Sim, Doheum Kim, Jeong Yeon Sim and SangYoun Park
Crystals 2017, 7(10), 296; https://doi.org/10.3390/cryst7100296 - 02 Oct 2017
Viewed by 4517
Abstract
The genes encoding three coiled-coil regions in human pericentrin were gene synthesized with Escherichia coli codon-optimization, and the proteins were successfully over-produced in large quantities using E. coli expression. After verifying that the purified proteins were mostly composed of α-helices, one of the [...] Read more.
The genes encoding three coiled-coil regions in human pericentrin were gene synthesized with Escherichia coli codon-optimization, and the proteins were successfully over-produced in large quantities using E. coli expression. After verifying that the purified proteins were mostly composed of α-helices, one of the proteins was crystallized using polyethylene glycol 8000 as crystallizing agent. X-ray diffraction data were collected to 3.8 Å resolution under cryo-condition using synchrotron X-ray. The crystal belonged to space group C2 with unit cell parameters a = 324.9 Å, b = 35.7 Å, c = 79.5 Å, and β = 101.6˚. According to Matthews’ coefficient, the asymmetric unit may contain up to 12 subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 1.96 Å3 Da−1 and a 37.3% solvent content. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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5735 KiB  
Article
Size and Shape Controlled Crystallization of Hemoglobin for Advanced Crystallography
by Ayana Sato-Tomita and Naoya Shibayama
Crystals 2017, 7(9), 282; https://doi.org/10.3390/cryst7090282 - 20 Sep 2017
Cited by 7 | Viewed by 9532
Abstract
While high-throughput screening for protein crystallization conditions have rapidly evolved in the last few decades, it is also becoming increasingly necessary for the control of crystal size and shape as increasing diversity of protein crystallographic experiments. For example, X-ray crystallography (XRC) combined with [...] Read more.
While high-throughput screening for protein crystallization conditions have rapidly evolved in the last few decades, it is also becoming increasingly necessary for the control of crystal size and shape as increasing diversity of protein crystallographic experiments. For example, X-ray crystallography (XRC) combined with photoexcitation and/or spectrophotometry requires optically thin but well diffracting crystals. By contrast, large-volume crystals are needed for weak signal experiments, such as neutron crystallography (NC) or recently developed X-ray fluorescent holography (XFH). In this article, we present, using hemoglobin as an example protein, some techniques for obtaining the crystals of controlled size, shape, and adequate quality. Furthermore, we describe a few case studies of applications of the optimized hemoglobin crystals for implementing the above mentioned crystallographic experiments, providing some hints and tips for the further progress of advanced protein crystallography. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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2017 KiB  
Article
Phenomenological Consideration of Protein Crystal Nucleation; the Physics and Biochemistry behind the Phenomenon
by Christo N. Nanev
Crystals 2017, 7(7), 193; https://doi.org/10.3390/cryst7070193 - 27 Jun 2017
Cited by 12 | Viewed by 4233
Abstract
Physical and biochemical aspects of protein crystal nucleation can be distinguished in an appropriately designed experimental setting. From a physical perspective, the diminishing number of nucleation-active particles (and/or centers), and the appearance of nucleation exclusion zones, are two factors that act simultaneously and [...] Read more.
Physical and biochemical aspects of protein crystal nucleation can be distinguished in an appropriately designed experimental setting. From a physical perspective, the diminishing number of nucleation-active particles (and/or centers), and the appearance of nucleation exclusion zones, are two factors that act simultaneously and retard the initially fast heterogeneous nucleation, thus leading to a logistic time dependence of nuclei number density. Experimental data for protein crystal (and small-molecule droplet) nucleation are interpreted on this basis. Homogeneous nucleation considered from the same physical perspective reveals a difference—the nucleation exclusion zones lose significance as a nucleation decelerating factor when their overlapping starts. From that point on, a drop of overall system supersaturation becomes the sole decelerating factor. Despite the different scenarios of both heterogeneous and homogeneous nucleation, S-shaped time dependences of nuclei number densities are practically indistinguishable due to the exponential functions involved. The biochemically conditioned constraints imposed on the protein crystal nucleation are elucidated as well. They arise because of the highly inhomogeneous (patchy) protein molecule surface, which makes bond selection a requisite for protein crystal nucleation (and growth). Relatively simple experiments confirm this assumption. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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Review

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987 KiB  
Review
Biomineralization Mediated by Ureolytic Bacteria Applied to Water Treatment: A Review
by Dayana Arias, Luis A. Cisternas and Mariella Rivas
Crystals 2017, 7(11), 345; https://doi.org/10.3390/cryst7110345 - 17 Nov 2017
Cited by 46 | Viewed by 8176
Abstract
The formation of minerals such as calcite and struvite through the hydrolysis of urea catalyzed by ureolytic bacteria is a simple and easy way to control mechanisms, which has been extensively explored with promising applications in various areas such as the improvement of [...] Read more.
The formation of minerals such as calcite and struvite through the hydrolysis of urea catalyzed by ureolytic bacteria is a simple and easy way to control mechanisms, which has been extensively explored with promising applications in various areas such as the improvement of cement and sandy materials. This review presents the detailed mechanism of the biominerals production by ureolytic bacteria and its applications to the wastewater, groundwater and seawater treatment. In addition, an interesting application is the use of these ureolytic bacteria in the removal of heavy metals and rare earths from groundwater, the removal of calcium and recovery of phosphate from wastewater, and its potential use as a tool for partial biodesalination of seawater and saline aquifers. Finally, we discuss the benefits of using biomineralization processes in water treatment as well as the challenges to be solved in order to reach a successful commercialization of this technology. Full article
(This article belongs to the Special Issue Biological and Biogenic Crystallization)
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