Special Issue "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)

Special Issue Editor

Guest Editor
Prof. Dr. Jolanta Prywer

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

Special Issue Information

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

Manuscript Submission Information

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Keywords

  • biological crystals
  • biogenic crystals
  • bio-inspired crystallization

Published Papers (5 papers)

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Research

Open AccessArticle Formation Mechanism of CaCO3 Spherulites in the Myostracum Layer of Limpet Shells
Crystals 2017, 7(10), 319; doi:10.3390/cryst7100319 (registering DOI)
Received: 14 August 2017 / Revised: 16 October 2017 / Accepted: 16 October 2017 / Published: 23 October 2017
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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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Open AccessFeature PaperArticle Modulating Nucleation by Kosmotropes and Chaotropes: Testing the Waters
Crystals 2017, 7(10), 0302; doi:10.3390/cryst7100302
Received: 24 August 2017 / Accepted: 4 October 2017 / Published: 6 October 2017
PDF Full-text (1391 KB) | HTML Full-text | XML Full-text | Supplementary Files
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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Open AccessCommunication Over-Production, Crystallization, and Preliminary X-ray Crystallographic Analysis of a Coiled-Coil Region in Human Pericentrin
Crystals 2017, 7(10), 296; doi:10.3390/cryst7100296
Received: 12 September 2017 / Revised: 27 September 2017 / Accepted: 28 September 2017 / Published: 2 October 2017
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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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Open AccessArticle Size and Shape Controlled Crystallization of Hemoglobin for Advanced Crystallography
Crystals 2017, 7(9), 282; doi:10.3390/cryst7090282
Received: 6 September 2017 / Revised: 16 September 2017 / Accepted: 17 September 2017 / Published: 20 September 2017
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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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Open AccessArticle Phenomenological Consideration of Protein Crystal Nucleation; the Physics and Biochemistry behind the Phenomenon
Crystals 2017, 7(7), 193; doi:10.3390/cryst7070193
Received: 23 May 2017 / Revised: 19 June 2017 / Accepted: 21 June 2017 / Published: 27 June 2017
Cited by 1 | PDF Full-text (2017 KB) | HTML Full-text | XML Full-text
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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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Different Nucleation Pathways for Protein Crystals
Authors: A.E.S. Van Driessche and M. Sleutel

Title: Formation Mechanism of CaCO3 Spherulites in Myostracum Layer of Limpet Shells
Authors: Shitao Wu, Chang-Yang Chiang and Wuzong Zhou
Affiliation: School of Chemistry, University of St Andrews, St Andrews, Fife KY16 9ST, United Kingdom
Abstract: CaCO3 (The phase to be determined) spherulites were found in the myostracum layer of common limpet shells. Their microstructures were revealed by using scanning electron microscopy, high resolution transmission electron microscopy, and energy dispersive X-ray microanalysis. Mechanisms of the formation of these spherulites and their morphology evolution were proposed in several steps, (1) formation of spherical particles of an inorganic and biological composite; (2) growth of CaCO3 nanorods on the surface of a core sphere; (3) formation of a core twin crystal; and (4) particle splitting into two hemispheres. It is believed that dipolar field of CaCO3 is the principal driving force for the orientated growth.

 

 

 

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