Cobalt-containing catalytic systems alloyed with rare and rare-earth metals as catalysts for synthesis of hydrocarbons from CO and H<Subscript>2</Subscript>

To improve cobalt-containing catalytic systems for synthesis of hydrocarbons from carbon monoxide and hydrogen (Fischer-Tropsch synthesis), supports based on ultradispersed alloys of aluminum with rare and rare-earth metals (G, Ce, Sm) were obtained and studied. The catalytic activity parameters of the new catalysts were determined.     

Compensation for Aberrations of Focused Ultrasound Beams in Transcranial Sonications of Brain at Different Depths

Acoustical Physics - The study analyzes the possibilities of compensating for aberrations when focusing an ultrasound beam through the skull bones using arrays with mosaic pattern of elements,...     

Three-dimensional structure of phosphopantetheine adenylyltransferase from <Emphasis Type="Italic">Mycobacterium tuberculosis</Emphasis> in the apo form and in complexes with coenzyme A and dephosphocoenzyme A

Crystals of phosphopantetheine adenylyltransferase (PPAT) from Mycobacterium tuberculosis in the apo form and in complexes with coenzyme A (PPAT/CoA) and dephosphocoenzyme A (PPAT/dPCoA) were grown in microgravity by the capillary counter-diffusion method. The structures of PPAT Mt in the apo form and in complexes with ligands were solved based on the X-ray diffraction data collected from the grown crystals. The crystal structures were refined at 1.76, 1.59, and 1.59 Å resolution to Rf factors of 0.175, 0.159, and 0.157 and Rfree of 0.224, 0.208, and 0.206 for PPAT, PPAT/CoA, and PPAT/dPCoA, respectively. The atomic coordinates of the structures were deposited in the Protein Data Bank (PDB ID: 3RFF, 3RHS, and 3RBA). In these structures, the ligand-binding sites were determined, the environment of these sites was characterized, and the conformational changes accompanying the ligand binding were analyzed.     

Crystal growth of phosphopantetheine adenylyltransferase,carboxypeptidase t,and thymidine phosphorylase on the international space station by the capillary counter-diffusion method

Crystals of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis, thymidine phosphorylase from Escherichia coli, carboxypeptidase T from Thermoactinomyces vulgaris and its mutant forms, and crystals of complexes of these proteins with functional ligands and inhibitors were grown by the capillary counter-diffusion method in the Japanese Experimental Module Kibo on the International Space Station. The high-resolution X-ray diffraction data sets suitable for the determination of high-resolution three-dimensional structures of these proteins were collected from the grown crystals on the SPring-8 synchrotron radiation facility. The conditions of crystal growth for the proteins and the data-collection statistics are reported. The crystals grown in microgravity diffracted to a higher resolution than crystals of the same proteins grown on Earth.     

Temperature-programmed reduction of cobalt-containing catalysts of the Fischer-Tropsch synthesis based on ultrafine aluminum powders alloyed with rare-earth metals

Russian Chemical Bulletin - The ultrafine aluminum powder alloyed with rare-earth metals (Ce, Sm), which is used as a support for the cobalt-containing catalysts of the Fischer-Tropsch synthesis,...     

Preparation of the Crystal Complex of Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis with Coenzyme A and Investigation of Its Three-Dimensional Structure at 2.1-Å Resolution

Crystallography Reports - Recombinant phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis (PPAT Mt), which was produced by a high-producing strain and purified to 99%, was used...