Protein Crystallography: The State of the Art

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

Deadline for manuscript submissions: 20 August 2024 | Viewed by 558

Special Issue Editors


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Guest Editor
Laboratory for Structural Biology of Infection and Inflammation, Department of Chemistry, Institute of Biochemistry and Molecular Biology, Universität Hamburg, Build. 22a, c/o DESY, 22607 Hamburg, Germany
Interests: structural biology; membrane proteins; SARS-CoV-2; mechanistic enzymology; structure-based drug discovery; time-resolved serial crystallography
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Guest Editor
1. ANSTO, Australian Synchrotron, 800 Blackburn Road, Clayton 3168, Australia
2. Department of Molecular Biology and Biochemistry, Monash University, Clayton 3800, Australia
Interests: structural biology; graphene-based biosensors; structural determination of macromolecules; software development in crystallography

Special Issue Information

Dear Colleagues,

X-ray diffraction is a prime technique to reveal the three-dimensional structures of biological molecules (proteins, metallo-enzymes, viruses and nucleic acids) at an atomic resolution of ~1.3 Å. Static structural information has been used to reveal the detailed mechanisms through which these molecules carry out their functions. Recent technical developments have made it possible to observe the structural dynamics of macromolecules and their complexes using various diffraction techniques available in third- or fourth-generation synchrotron sources.

We invite researchers to contribute to this Special Issue on “Protein Crystallography: the State of the Art”, which is intended to serve as a unique forum covering broad aspects of the current status of time-resolved serial crystallography in XFEL and in synchrotrons, pink beam crystallography and its progress and prospects in the field of mechanistic enzymology, structural-based drug discovery, an understanding of macromolecular complexes and membrane proteins as well as future software developments for macromolecular crystallography, and crystallization and complementary techniques (i.e., SAXS, NMR, spectroscopic techniques). We accept research articles, reviews and short communications.

Dr. Vasundara Srinivasan
Dr. Santosh Panjikar
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 submissions that pass pre-check are 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 2600 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

  • time-resolved serial crystallography in XFEL and synchrotrons (TR-SFX, TR-SSX)
  • pink beam crystallography
  • small-angle X-ray scattering (SAXS)
  • structural-based drug discovery
  • mechanistic enzymology
  • membrane proteins
  • macromolecular complexes
  • software developments for macromolecular crystallography
  • deep learning and artificial intelligence

Published Papers (1 paper)

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Research

15 pages, 3992 KiB  
Article
The Dynamical Properties of Three Different Variants of the Orange Carotenoid Protein: A Quasielastic Neutron Scattering Study
by Mina Hajizadeh, Maksym Golub, Marcus Moldenhauer, Wiebke Lohstroh, Thomas Friedrich and Jörg Pieper
Crystals 2024, 14(4), 361; https://doi.org/10.3390/cryst14040361 - 11 Apr 2024
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Abstract
Besides a well-adapted structure, proteins often require a specific dynamical flexibility to undergo conformational changes in order to carry out their function. The latter dynamics can be directly measured by quasielastic neutron scattering as demonstrated here for three variants of the orange carotenoid [...] Read more.
Besides a well-adapted structure, proteins often require a specific dynamical flexibility to undergo conformational changes in order to carry out their function. The latter dynamics can be directly measured by quasielastic neutron scattering as demonstrated here for three variants of the orange carotenoid protein (OCP), which plays a pivotal role in the protection of the cyanobacterial photosynthetic apparatus against photodamage. We investigate the dynamics of the structurally compact, dark-adapted wild type of OCP (OCPwt) in comparison with that of two mutant forms. The latter two mutants differ preferentially in their structures. The orange mutant OCP-W288A is assumed to have a compact structure and to preferentially bind the pigment echinenone, while the pink mutant OCP-W288A appears to represent the more elongated structure of the red active state of OCP binding the carotenoid canthaxanthin, respectively. The study reveals three major findings: (a) the dynamics of the red active state of OCP is significantly enhanced due to a larger number of protein residues being exposed to the solvent at the surface of the protein; (b) the dynamics of all OCP forms appear to be suppressed upon the freezing of the solvent, which is most likely due to an ice-induced aggregation of the proteins; and (c) the wild type and the compact mutant exhibit different dynamics attributed to a missing H-bond between the pigment and protein, resulting a destabilization of the surrounding protein. Full article
(This article belongs to the Special Issue Protein Crystallography: The State of the Art)
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