Di-μ-benzoato-di-μ-ethano-lato-tetra-kis-[μ-5-(hy-droxy-meth-yl)-2-methyl-4-(oxidometh-yl)pyridin-1-ium-3-olato]tetra-kis-[μ-5-(hy-droxy-meth-yl)-2-methyl-4-(oxidometh-yl)pyridin-3-olato]di-μ-oxido-hepta-manganese(II,III) ethanol octa-solvate.

Our work in the area of synthesis of polynuclear manganese complexes and their magnetic properties led to the synthesis and crystallization of the title compound, [Mn(CHNO)(CHNO)(CHO)(CHO)O]·8CHOH. Herein, we report the molecular and crystal structure of the title compound, which was synthesized by the reaction of Mn(CHCOO) with pyridoxine (PNH, CHNO) followed by the addition of tetra-methyl-ammonium hydroxide (TMAOH). The core of this centrosymmetric complex is a cage-like structure consisting of six Mn ions and one Mn ion bound together through Mn-O bonds.

Crystal structure and Hirshfeld surface analysis of the elusive trichlorobis(diethyl ether)oxomolybdenum(V).

First reported in 1930, MoClO(EtO) is a by-product of the reductive synthesis of MoCl(OEt) from MoCl. We report herein the X-ray crystal structure and Hirshfeld surface characteristics of mer-MoClO(EtO), or [MoClO(CHO)]. The compound crystallizes in the orthorhombic space group P222.

Catalytic intramolecular hydroamination of aminoallenes using titanium complexes of chiral, tridentate, dianionic imine-diol ligands.

Alkylation of d- or l-phenylalanine or valine alkyl esters was carried out using methyl or phenyl Grignard reagents. Subsequent condensation with salicylaldehyde, 3,5-di-tert-butylsalicylaldehyde, or 5-fluorosalicylaldehyde formed tridentate, X2L type, Schiff base ligands. Chiral shift NMR confirmed retention of stereochemistry during synthesis.

The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site.

We report the crystal structure of alanine racemase from Mycobacterium tuberculosis (Alr(Mtb)) at 1.9 A resolution. In our structure, Alr(Mtb) is found to be a dimer formed by two crystallographically different monomers, each comprising 384 residues.

Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms.

The structure of the catabolic alanine racemase, DadX, from the pathogenic bacterium Pseudomonas aeruginosa, reported here at 1.45 A resolution, is a dimer in which each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the PLP cofactor and a second domain primarily composed of beta-strands. The geometry of each domain is very similar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains differs by about 15 degrees.

Characterization and crystallization of active domains of a novel luciferase from a marine dinoflagellate.

Lingulodinium polyedrum luciferase is a bioluminescent protein found in the marine dinoflagellate formerly known as Gonyaulax. It is located in organelles called scintillons that emit brief and bright flashes of light that are regulated by an endogenous circadian clock. The complete luciferase molecule has a molecular mass of 136 994 Da and contains three homologous domains, each of which is a separately active luciferase.

The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation.

Crystallographic studies revealing the three-dimensional structure of the oxidized form of the [2Fe-2S] ferredoxin from Trichomonas vaginalis (TvFd) are presented. TvFd, a member of the hydrogenosomal class of ferredoxins, possesses a unique combination of redox and spectroscopic properties, and is believed to be the biological molecule that activates the drug metronidazole reductively in the treatment of trichomoniasis. It is the first hydrogenosomal ferredoxin to have its structure determined.