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 cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of ruminant specific galectin-11 is described
Synopsis: Crystals of the N-terminal domain of nucleocapsid protein from Middle East respiratory syndrome coronavirus that diffracted X-rays to a resolution of at least 2.63 Å.
Synopsis: The crystal structure of the Human MLH1 N-terminus is reported at 2.30 Å. The overall structure is described along with an analysis of two clinically important mutations.
Synopsis: The preliminary structural analysis of marine phycoerythrin is described, showing distinct sequence features.
Synopsis: A GH43 -xylosidase from the bacterium B. licheniformis was cloned, overexpressed in E. coli BL21(DE3) cells, purified and crystallized. The crystals belonged to the monoclinic space group C2 and diffracted to 2.49 Å resolution.
Synopsis: We present a new batch preparation method of high density micron-sized crystals of the G protein-coupled receptor (GPCR) rhodopsin for their use in time-resolved serial femtosecond crystallography (SFX) at a X-ray free electron laser (X-FEL) using a liquid jet.
Synopsis: The structure of the full-length response regulator ChrA in an unphosphorylated state revealed a unique linker conformation and an interdomain reorientation.
Synopsis: A putative carbohydrate-binding module from a modular family 5 glycoside hydrolase from R. flavefaciens FD-1 was purified and crystallized and data were collected from cacodylate-derivative crystals to 1.02 and 1.29 Å resolution.
Synopsis: A novel thermostable aldo-keto reductase Tm1743 from Thermotoga maritima was overexpressed with an N-terminal His6 tag, purified and co-crystallized with NADP+. Degradation of the N-terminal vector-derived amino acids was identified by Western blot and Mass Spectrometry analysis.
Synopsis: The cloning, purification, crystallization and preliminary X-ray diffraction studies of M. tuberculosis J are reported. M. tuberculosis J is an extracytoplasmic function factor that governs the cellular response to oxidative stress.
Synopsis: MORPHEUS II is a 96-condition initial crystallization screen formulated de novo. The screen incorporates reagents selected from the Protein Data Bank to yield crystals not observed in traditional conditions. In addition, the formulation facilitate optimization and cryoprotection of crystals.
Synopsis: Influence of fluorinated segment length on surfactant micelle form factors, intermicellar interaction parameters and surfactant phase diagram in solution conditions for MP crystallization.
Synopsis: The crystal structure of the recombinant prolidase from T. sibiricus was determined by X-ray diffraction to a resolution of 2.6 Å and deposited in the Protein Data Bank.
Synopsis: LJL143, a salivary protein from L. longipalpis, was produced using P. pastoris and crystallized in space group P212121.
Synopsis: The crystal structure of a functional C-terminal domain of human collapsin response mediator protein 1 has been determined at 3 Å resolution.
Synopsis: YdiE, a conserved protein apparently involved in haem transport, is one of the smallest proteins produced by E. coli at only 63 residues in length. The N-terminal 20 residues of each chain in the homodimer were disordered, but crystals of the full-length protein allowed structure refinement to 1.5 Å resolution.
Synopsis: An X-ray compatible microfluidic crystallization platform enables in situ time-resolved serial Laue crystallography.
Synopsis: We characterize the evolutions of protein-rich clusters and nucleating crystals by dynamic light scattering (DLS), confocal depolarized dynamic light scattering (cDDLS) and depolarized oblique illumination dark-field microscopy. Our observations indicate that the protein-rich clusters are locations for crystal nucleation, moreover we directly detect newly nucleated crystals within protein-rich clusters.
Synopsis: A novel aromatic prenyltransferase from A. terreus, named AtaPT, was found to prenylate diverse novel aromatic compounds. The expression and crystallization of AtaPT are reported here.
Synopsis: The expression, purification and crystal structure of a recombinant fluorobody to TLH are reported.
Synopsis: The crystal structure of mouse nerve growth factor (NGF) complexed with lysophosphatidylinositol was solved and the structural determinants of NGF for LysoPI molecule recognition were identified. The influence of LysoPI in the interactions between NGF and its two receptors is modelled.
Synopsis: The crystal structures of the individual domains of the Mex67-Mtr2 complex from C. thermophilum have been determined and their arrangement in solution has been studied by SAXS.
Synopsis: The presence of a covalently bound fluorescent probe at concentrations in the < 0.5% range do not affect the outcomes of macromolecule crystallization screening experiments. Additionally, the fluoresence can be used to determine new, not immediately apparent, lead crystallization conditions.
Synopsis: The C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2 (including residues Lys318-Arg416) was produced in E. coli, purified and crystallized, and X-ray diffraction data were collected to 2.10 Å resolution.
Synopsis: A 1.8 Å resolution structure of the sphingolipid activator protein saposin A has been determined at pH 4.8, the physiologically relevant lysosomal pH for hydrolase enzyme activation and lipid-transfer activity.
Synopsis: This article describes preliminary crystallographic data for the I26A/N52A mutant of nonstructural protein 15 from Human coronavirus 229E.
Synopsis: A. thaliana BAG5 (AtBAG5) and calmodulin were expressed and purified separately and then co-crystallized. The preliminary X-ray diffraction studies of the protein complex are reported in order to provide structural insights into the mode of interaction between AtBAG5 and calmodulin.
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