The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section F: Structural Biology and Crystallization Communications.
This list will generally be short, as papers in this journal are published online as soon as proofs are returned.
See also Forthcoming articles in all IUCr journals.
Synopsis: A -1,3-glucanase from the thermophilic fungus C. thermophilum was overexpressed in P. pastoris, purified and crystallized. In situ diffraction at synchrotron and seeding were used to obtain reproducible crystals. A complete data set to 2.0 Å resolution was collected using an in-house X-ray generator.
Synopsis: The CFA/III minor pilin subunit, CofB, was crystallized. An N-terminal hydrophobic portion of CofB was truncated to enable initial crystallization. Dehydration of preliminary crystals yielded higher resolution diffraction patterns.
Synopsis: Crystallization and diffraction studies of the HIRAN domain of human HLTF
Synopsis: Diffraction data from crystals of zebrafish (Danio rerio) 2-microglobulins type I and type II (Dare-2m-I and Dare-2m-II) were collected to 1.6 Å and 1.9 Å resolutions, respectively. Both crystals belonged to space group P212121, with unit-cell parameters a = 38.2 Å, b = 50.4 Å, c = 50.9 Å for Dare-2m-I, and a = 38.9, b = 52.7, c = 65.8 Å for Dare-2m-II. Each asymmetric unit contained one molecule. The Matthews coefficient and solvent content of Dare-2m-I and Dare-2m-II were calculated to 2.22 Å3 Da-1 and 45%, and 3.01 Å3 Da-1 and 59%, respectively.
Synopsis: Plasmodium falciparum orotate phosphoribosyl transferase (PfOPRTase), a potential target of antimalarial drugs and a conduit for prodrugs, crystalized as an 8-molecule per asymmetric unit structure (PDB id: 4fym) including some unique parasite-specific auto-inhibitory interactions between catalytic dimers.
Synopsis: The crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S) is presented at 1.67 Å resolution.
Synopsis: A review and historical perspective covering the many different aspects of antiparasitic drug discovery in particular targeting protists (hereafter called protozoa) is presented. The key role of structural studies in the process is highlighted and specific high-profile examples are given.
Synopsis: ADP-ribosylation factors (ARFs) are highly conserved proteins present in all Eukarya. The structure of ARF from E. histolytica is described and compared with orthologs from other species.
Synopsis: Superoxide dismutases (SODs) catalyze the conversion of superoxide to molecular oxygen, thus protecting organisms against toxic radicals. Iron-dependent SODs from T. cruzi, L. major and B. bovis exist as multiple isoforms with distinct structural features.
Synopsis: In this review, current structural understanding of the apicomplexan glideosome and actin regulation is described.
Synopsis: N-Myristoyltransferase (NMT) has been shown to be an attractive target for the development of novel therapeutic agents for the treatment of human African trypanosomiasis. A fragment library has been screened using NMR spectroscopy and the binding mode of hits was confirmed by X-ray crystallography using L. major NMT as a structural surrogate.
Synopsis: Hookworm platelet inhibitor belongs to the cysteine-rich/antigen-5/pathogenesis-related-1 (CAP) protein family. It has been linked with integrin-antagonist, antiplatelet activity found in extracts of A. caninum hookworms.
Synopsis: The production, purification and crystallization of a recently identified trans-sialidase from T. vivax is described. The purified enzyme is active and produces diffraction-quality crystals using the sitting-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffracted to 2.5 Å resolution.
Synopsis: Structures of the histidine triad family protein from E. histolytica were solved in complex with sulfate, AMP or GMP. The three structures show very similar nucleotide poses, with the sulfate occupying the same space as the -phosphate of the nucleotides.
Synopsis: Structures of aspartate aminotransferases from eukaryotic pathogens were solved in complex with pyridoxal phosphate. The four structures show either the open or the closed conformation of the enzyme. The structures highlight the challenges for structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm.
Synopsis: The X-ray structure of the antimalarial drug target dihydroorotate dehydrogenase bound to a potent and selective benzamide-based inhibitor shows novel binding-site interactions.
Synopsis: The crystal structure of L. (V.) braziliensis dihydroorotate dehydrogenase, a potential target for drug development against cutaneous leishmaniasis, is reported.
Synopsis: Compound P131 displays antiparasitic activity in a mouse model of Cryptosporidium infection, validating IMP dehydrogenase (IMPDH) as a drug target. Here, the structure of the enzyme-substrate-P131 complex is reported at 2.05 Å resolution. The structure is an important step to further refine the design of IMPDH inhibitors.
Synopsis: C. parvum is the primary protozoan parasite from the Cryptosporidium genus responsible for cryptosporidiosis in humans. Here, the 2.0 Å resolution structure of the divalent-cation tolerance protein CutA1 encoded in the genome of C. parvum Iowa II is described.
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