Special Issue "Recent Advances in Protein Crystallography"
Deadline for manuscript submissions: 31 December 2017
The field of the structural biology is thriving owing to several so-called “revolutions”, such as the advent of X-ray Free Electron Lasers, remarkable improvements in detectors’ resolution for Cryo-electron Microscopy and many other important developments in all aspects of the field: Protein expression, purification, crystallization, data processing and analysis, and so on. We decided to compile this Special Issue on “Recent advances in Protein Crystallography” to summarize the current progress and the state-of-the-art of the structural biology. Authors are encouraged to submit their manuscripts covering topics expressed in the keywords below. The additional goal of this issue is to provide the growing community of scientists interested in structural biology with an excellent reference material. Additionally we will compile the subsection on protein structures, thus manuscripts describing new structures with the structural-functional analysis or “old” structures but with a new twist are also welcome.
Dr. Albert Guskov
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 1000 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.
- Structural biology
- Protein crystallography
- Membrane proteins
- Protein crystallization
- X-ray Free Electron Laser
- Cryo-Electron Microscopy
- Protein Expression and purification
- Data processing and analysis
- Refinement and validation
- Biophysical characterization
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: Radiation Damage in Macromolecular Crystallography
Authors: Helena Taberman
Affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
Title: State-of-the Art Behavioral Characterizations of the PB2cap Binding Domain Accelerate Inhibitor Design
Authors: Amanda Constantinides, Chelsea Severin, Ryan Gummper, Xiaofeng Zheng and Ming Luo
Abstract: Influenza A and B’s evolutionary adaptations are no match for modern visualization technology. X-ray crystallographic structural determinations of Influenza A’s PB2 cap binding domain (PB2cap) have dynamically improved the behavioral characterization of Influenza’s RNA-dependent RNA polymerase machinery (PA, PB2, and PB1). Structurally resembling the human hand by the catalytic PB1 subunit, PA lies near the finger region, and PB2 lies near the thumb region. PB2 “cap-snatches” the host cell’s pre-mRNA, while PA’s endonuclease cuts it 10-13 nucleotides downstream and transfers it to PB1, where viral mRNA is synthesized (Tarendeau et al., 2007). Precisely targeting the PB2cap binding domain with a small molecule inhibitor will halt viral proliferation via interference with cap-snatching behavior. Unliganded wild-type, liganded, and unliganded mutant PB2cap from A/California/07/2009 H1N1 was expressed in Escherichia coli, purified by Nickel Affinity and Size Exclusion chromatography, crystallized, and subjected to X-ray diffraction experiments. Structures were solved by the molecular replacement method, refined, and deposited in the Protein Data Bank (PDB). Structural determinations revealed the functions of Glu361, Lys376, His357, Phe404, Phe323, Lys339, His432, Asn429, Gln406, and Met401 in the Influenza A PB2cap binding domain (Severin et al., 2016) and the dissociation of the Influenza A PB2cap C-terminal domain (residues 446-479) upon ligand binding (Constantinides et al., 2017). Understanding the behavior of these residues will aid in the ultimate development of a small-molecule inhibitor that binds both Influenza A and B PB2cap.
Title: High-resolution crystal structure of RpoS fragment including a partial region 1.2 and region 2 from the intracellular pathogen Legionella pneumophila
Authors: Nannan Zhang, Xiaofang Chen, Xiaojian Gong, Honghua Ge*
Affiliation: Institute of Health Sciences, Anhui University, Hefei, Anhui 230601, China
Abstract: Legionella pneumophila RpoS (LpRpoS) is an alternative sigma factor of RNA polymerase (RNAP) essential for virulence and stress resistance. To investigate the mechanism of RpoS in the intracellular pathogen L. pneumophila, we determined the high-resolution crystal structure of the LpRpoS (residues 95-194) containing a partial region 1.2 and region 2 at 1.6 A resolution. The structure reveals that the conserved residues are critical for promoter melting, DNA and core RNAP binding. The differences in regulatory factor binding sites between Escherichia coli RpoS and LpRpoS suggest that LpRpoS may employ a distinct mechanism to recruit alternative regulatory factors controlling transcription initiation.