Advanced Technologies for Analysis, Directed Optimization and Delivery of Protein 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 2019)

Special Issue Editors

Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, Notkestrasse 85, c/o DESY, Build. 22a, 22603 Hamburg, Germany
Interests: nucleation in protein crystallization; x-ray crystallography and molecular modeling; multicrystal diffraction; structural infection biology crystallogenesis structure; dynamics of nucleic acids specific plant lectins venom proteomics
Special Issues, Collections and Topics in MDPI journals
President of the International Organization for Biological Crystallization (IOBCr)
Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Germany
Interests: macromolecular crystallography; structural infection biology; crystallogenesis; optimization; automation; crystallography teaching

Special Issue Information

Dear Colleagues,

Over the last few years, the establishment and continuous development of Serial Femtosecond Crystallography (SFX) at X-ray Free Electron Laser (XFEL) Radiation Sources and the establishment of Serial Crystallography (SX) at most high brilliant synchrotron radiation (SR) sources indicate that the methods and procedures used in protein crystallography, from single crystals to well-defined suspensions of crystals, has changed substantially and will continue to do so for the next decade. The latest serial diffraction data collection methods, including crystal delivery procedures, emphasize current efforts to develop new and efficient procedures to produce protein microx- and nano-crystals, including the challenge of preparing and scoring crystalline suspensions to meet particular crystal delivery methods at XFEL and SR beamlines. This Special Issue aims to summarize and provide insight regarding the latest methods in crystallogenesis to produce micro- and nano-sized crystals, besides conventional single crystal production, in vitro and in vivo. Further, particular methods to characterize crystalline suspensions will be included. In summary, this Special Issue will be of interest for crystal growth experts, as well as for young scientist and scholars interested in the field.

Prof. Dr. Christian Betzel
Dr. Jeroen R. Mesters
Guest Editors

Manuscript Submission Information

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Keywords

  • Distinct crystals growth
  • In-vivo crystallization
  • Crystal nucleation and liquid dense protein clusters
  • Crystal growth for neutron diffraction
  • External electrical and magnetic fields
  • Microgravity crystallization
  • Mass transport in crystallization
  • In situ analysis of crystals
  • In situ optimization of crystals
  • Physicochemical characterization of crystals
  • Scoring crystal suspensions
  • Instrument and software development
  • Crystal delivery for XFEL and Synchrotron radiation sources

Published Papers (4 papers)

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Research

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14 pages, 2263 KiB  
Article
Multi-Step Concanavalin A Phase Separation and Early-Stage Nucleation Monitored Via Dynamic and Depolarized Light Scattering
by Hévila Brognaro, Sven Falke, Celestin Nzanzu Mudogo and Christian Betzel
Crystals 2019, 9(12), 620; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst9120620 - 26 Nov 2019
Cited by 6 | Viewed by 3346
Abstract
Protein phase separation and protein liquid cluster formation have been observed and analysed in protein crystallization experiments and, in recent years, have been reported more frequently, especially in studies related to membraneless organelles and protein cluster formation in cells. A detailed understanding about [...] Read more.
Protein phase separation and protein liquid cluster formation have been observed and analysed in protein crystallization experiments and, in recent years, have been reported more frequently, especially in studies related to membraneless organelles and protein cluster formation in cells. A detailed understanding about the phase separation process preceding liquid dense cluster formation will elucidate what has, so far, been poorly understood—despite intracellular crowding and phase separation being very common processes—and will also provide more insights into the early events of in vitro protein crystallization. In this context, the phase separation and crystallization kinetics of concanavalin A were analysed in detail, which applies simultaneous dynamic light scattering and depolarized dynamic light scattering to obtain insights into metastable intermediate states between the soluble phase and the crystalline form. A multi-step mechanism was identified for ConA phase separation, according to the resultant ACF decay, acquired after an increase in the concentration of the crowding agent until a metastable ConA gel intermediate between the soluble and final crystalline phases was observed. The obtained results also revealed that ConA is trapped in a macromolecular network due to short-range intermolecular protein interactions and is unable to transform back into a non-ergodic solution. Full article
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8 pages, 1165 KiB  
Article
Extending the pool of compatible peptide hydrogels for protein crystallization
by Guillermo Escolano-Casado, Rafael Contreras-Montoya, Mayte Conejero-Muriel, Albert Castellví, Judith Juanhuix, Modesto T. Lopez-Lopez, Luis Álvarez de Cienfuegos and José A. Gavira
Crystals 2019, 9(5), 244; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst9050244 - 10 May 2019
Cited by 3 | Viewed by 3262
Abstract
Short-peptide supramolecular (SPS) hydrogels are a class of materials that have been found to be useful for (bio)technological applications thanks to their biocompatible nature. Among the advantages reported for these peptides, their economic affordability and easy functionalization or modulation have turned them into [...] Read more.
Short-peptide supramolecular (SPS) hydrogels are a class of materials that have been found to be useful for (bio)technological applications thanks to their biocompatible nature. Among the advantages reported for these peptides, their economic affordability and easy functionalization or modulation have turned them into excellent candidates for the development of functional biomaterials. We have recently demonstrated that SPS hydrogels can be used to produce high-quality protein crystals, improve their properties, or incorporate relevant materials within the crystals. In this work, we prove that hydrogels based on methionine and tyrosine are also good candidates for growing high-quality crystals of the three model proteins: lysozyme, glucose isomerase, and thaumatin. Full article
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13 pages, 1593 KiB  
Article
The Study of the Mechanism of Protein Crystallization in Space by Using Microchannel to Simulate Microgravity Environment
by Yong Yu, Kai Li, Hai Lin and Ji-Cheng Li
Crystals 2018, 8(11), 400; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst8110400 - 24 Oct 2018
Cited by 3 | Viewed by 4119
Abstract
Space is expected to be a convection-free, quiescent environment for the production of large-size and high-quality protein crystals. However, the mechanisms by which the diffusion environment in space improves the quality of the protein crystals are not fully understood. The interior of a [...] Read more.
Space is expected to be a convection-free, quiescent environment for the production of large-size and high-quality protein crystals. However, the mechanisms by which the diffusion environment in space improves the quality of the protein crystals are not fully understood. The interior of a microfluidic device can be used to simulate a microgravity environment to investigate the protein crystallization mechanism that occurs in space. In the present study, lysozyme crystals were grown in a prototype microchannel device with a height of 50 μm in a glass-polydimethylsiloxane (PDMS)-glass sandwich structure. Comparative experiments were also conducted in a sample pool with a height of 2 mm under the same growth conditions. We compared the crystal morphologies and growth rates of the grown crystals in the two sample pools. The experimental results showed that at very low initial supersaturation, the morphology and growth rates of lysozyme crystals under the simulated microgravity conditions is similar to that on Earth. With increasing initial supersaturation, a convection-free, quiescent environment is better for lysozyme crystal growth. When the initial supersaturation exceeded a threshold, the growth of the lysozyme crystal surface under the simulated microgravity conditions never completely transform from isotropic to anisotropic. The experimental results showed that the convection may have a dual effect on the crystal morphology. Convection can increase the roughness of the crystal surface and promote the transformation of the crystal form from circular to tetragonal during the crystallization process. Full article
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Review

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7 pages, 969 KiB  
Review
Choosing the Method of Crystallization to Obtain Optimal Results
by Lata Govada and Naomi E. Chayen
Crystals 2019, 9(2), 106; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst9020106 - 19 Feb 2019
Cited by 9 | Viewed by 10625
Abstract
Anyone who has ever attempted to crystallise a protein or other biological macromolecule has encountered at least one, if not all of the following scenarios: No crystals at all, tiny low quality crystals; phase separation; amorphous precipitate and the most frustrating; large, beautiful [...] Read more.
Anyone who has ever attempted to crystallise a protein or other biological macromolecule has encountered at least one, if not all of the following scenarios: No crystals at all, tiny low quality crystals; phase separation; amorphous precipitate and the most frustrating; large, beautiful crystals that do not diffract at all. In this paper we review a number of simple ways to overcome such problems, which have worked well in our hands and in other laboratories. It brings together information that has been dispersed in various publications and lectures over the years and includes further information that has not been previously published. Full article
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