Special Issue "Advances in Protein Crystallization and Crystallography"
Deadline for manuscript submissions: 31 December 2021.
Interests: crystallization of biological macromolecules; conventional; advanced and alternative crystallization techniques; protein crystals; crystal structures; structural and modeling studies
Interests: protein crystallization; protein crystallography; enzymes, protein-DNA complexes
The crystallization of biological macromolecules is still poorly understood and, as a consequence, the success of common trial-and-error experiments is not very predictable. On the other hand, more rational approaches have been developed in the past years, and prospects for the science are in fact good. The topics of the Special Issue are aimed to cover all aspects of biological crystallization and crystallography from basic research on nucleation and crystal growth, to practical developments in crystallization methods and also advanced approaches and new protein crystal structures. New trends and methodologies as well as other structural methods will be encouraged.
Prof. Ivana Kuta Smatanova
Prof. Pavlína Maloy Řezáčová
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 1800 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.
- Crystallization of biological macromolecules
- Conventional techniques and their modifications
- Advanced and alternative crystallization methods
- Crystals of membrane and soluble proteins
- Crystals of protein–nucleic acid complexes
- Crystals for XFEL
- Intracellular protein crystallization
- Evaluation of crystallization trials
- Practical crystallography
- Crystal structures
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: Ionic Liquids as Protein Crystallization Additives
Authors: Crissy L. Tarver; Qunying Yuan; Marc L. Pusey
Affiliation: Dept. of Structural Biology, Stanford University School of Medicine, Palo Alto, CA, USA Dept. of Biological and Environmental Science, Alabama A & M University, Normal, AL, USA Dept. of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35805, USA
Abstract: Among its attributes, the mythical philosopher’s stone is supposedly capable of turning base metals to gold or silver. In an analogous fashion, we are finding that protein crystallization optimization using ionic liquids (ILs) often results in the conversion of base protein precipitate to crystals. Recombinant inorganic pyrophosphatases from pathogenic bacteria as well as several model proteins were tested for optimization by 23 ILs, plus a dH2O control, at IL concentrations of 0.1, 0.2, and 0.4 M. The IL’s were used as additives, and all proteins crystallized in the presence of at least one IL. For 9 of the 10 proteins precipitation conditions were converted to crystals with at least one IL. The ILs could be ranked in order of effectiveness, and it was found that ~90% of the crystallization conditions could be obtained with a suite of just 8 ILs, with the top two ILs accounting for slightly over 50% of the hits. Structural trends were found in the effectiveness of the ILs, with shorter alkyl chain ILs being more effective than longer. Curiously however a butyl group was present on the cation of three of the top eight ILs.
Title: Molecular composition of native (non-linked) CD160-HVEM protein complex revealed by initial crystallographic analysis
Authors: Lenhartova, S.
Affiliation: Department of Viral Immunology, Biomedical Research Center of the Slovak Academy of Sciences, Bratislava, Slovakia
Abstract: An increasing number of surface-exposed ligands and receptors acting on immune cells are being considered as a starting point in drug development applications. As they are dedicated to manipulate a wide range of immune responses, accurately predicting their molecular interactions will be necessary for the development of safe and effective therapeutics to enhance immune responses and vaccination. Here, we focused on characterization of human CD160 and HVEM immune receptors that contribute to T cell inhibition, natural killer cell activation, or mucosal immunity; and their mutual engagement leads to bidirectional signaling. In particular, our study report on the molecule preparation, characterization and initial crystallographic analysis of CD160-HVEM complex and both HVEM and CD160 alone. Despite the importance of the CD160-HVEM immune signaling and its therapeutic relevance, the structural and mechanistic basis underlying CD160-HVEM engagement has some controversial evidence. Some newer studies reported CD160 molecule in monomeric form (Liu, 2019; Kojima, 2011; Stiles, 2010), while older reports provided evidence on multimeric form acting on immune cells (Anumanthan, 1998; Maiza, 1993). In our study, the native CD160-HVEM complex (without linker) was co-expressed in the baculovirus-insect host; purified to homogeneity by anion-exchange chromatography to provide missing evidence of trimeric form in solution. The CD160-HVEM crystallized in space group P213 with unit cell parameters that could accommodate one trimeric complex in asymmetric unit. Crystals of CD160-HVEM complex, CD160 trimer and HVEM monomer diffracted to a minimum Bragg spacing of 2.8, 3.1 and 1.9 Å resolution respectively.