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: The X-ray crystal structure of the enteropathogenic Escherichia coli gatekeeper protein SepL has three X-bundle domains.
Synopsis: The structure has been determined at 2.3 Å resolution of the - hetero-dimer of the F-ATPase from the -proteobacterium, Paracoccus denitrificans. It corresponds to the "open" or "empty" catalytic interface found in other F-ATPases.
Synopsis: We have extended the resolution of the structure of the enzyme 2,4'-dihydroxyacetophenone dioxygenase to 1.88 Å and demonstrated by gel-filtration and analytical ultracentrifugation that in-situ chymotrypsinolysis, which is required for crystallization, converts the enzyme from a tetrameric to a dimeric form. A putative model of the tetramer obtaining by symmetric docking studies closely resembles the tetrameric assembly of the homologous rmlc-like cupin protein from R. eutropha: 3ebr.
Synopsis: Citrate synthase from the thermophilic euryarchaeon Thermoplasma acidophilum, fused to a hexahistidine tag, was purified and biochemically characterized. The structure of the unliganded enzyme at 2.2 Å resolution contains tail-active site contacts in half of the active sites.
Synopsis: Crystallization and preliminary data collection to 2.2 Å for the C1 protein of salmonella phage P22 as a complex with a 23-mer DNA is reported.
Synopsis: The crystal structure of the HECT domain of WWP2, an E3 ubiquitin-protein ligase, has been determined at 2.5 Å resolution and reveals a compact inverted "T" shape conformation.
Synopsis: RAB11(S20V), a constitutively active GTP-binding form of RAB1 1, was purified and crystallized. The crystals belong to space group I4 with unit-cell parameters of a = 74.11, b = 74.11, c = 149.44 Å. They were obtained at 293 K and diffracted to a resolution of 2.4 Å.
Synopsis: KDM5B is an important new putative cancer therapy target. Here we describe the binding properties and crystal structure of a nanobody raised against KDM5B.
Synopsis: The antibacterial compound QPT-1, the antibacterial drug moxifloxacin and the anticancer drug etoposide were each co-crystallized with DNA and S. aureus DNA gyrase. The base pairs at the ends of DNA duplexes were modified to optimize the crystal contacts and to give diffraction data to between 2.45 and 3.15 Å resolution from six DNA-complex crystals.
Synopsis: Frutalin, an -D-galactose-binding lectin of biomedical interest from A. incisa seeds, has been crystallized and its preliminary X-ray diffraction analysis at 1.81 Å resolution is reported.
Synopsis: In a large-scale study using data from the Protein Data Bank, some of the many reported findings regarding the crystallization of proteins were investigated.
Synopsis: Csm2 is a major component of type IIIA CRISPR ribonucleoprotein complexes that confer prokaryotes with immunity against phages and plasmids via an RNA-guided interference mechanism. The Csm2 protein from T. maritima was recombinantly expressed, purified and crystallized, and its structure was solved via cadmium single-wavelength anomalous diffraction phasing.
Synopsis: The crystal structure of the response regulator RPA3017 from the photosynthetic bacterium R. palustris has been determined at 1.9 Å resolution. RPA3017 is part of a two-component system that involves two tandem bacteriophytochromes involved in red-light signaling.
Synopsis: The anthracycline-biosynthetic enzyme DnmZ has been structurally characterized in ligand-free and thymidine diphosphate-bound forms.
Synopsis: Over 250 proteins have been subjected to a standard dye-based thermal melt analysis, and the results suggest that at least a third of soluble protein samples can be made significantly more stable by changing the composition of their formulation.
Synopsis: An engineered human carbonic anhydrase IX (CA IX) mimic was co-crystallized with the disaccharide sucrose. Its binding provides a novel `interaction' site that can be used to design targeted inhibitors of CA IX, a key marker of hypoxic tumors.
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