ABSTRACT
Advancements in computer-controlled polishing, metrology, and replication have led to an x-ray mirror fabrication process that is capable of producing high-resolution Wolter microscopes. We present the fabrication and test of a nickel-cobalt replicated full-shell x-ray mirror that was electroformed from a finely figured and polished mandrel. This mandrel was designed for an 8-m source-to-detector-distance microscope, with 10× magnification, and was optimized to reduce shell distortions that occur within 20 mm of the shell ends. This, in combination with an improved replication tooling design and refined bath parameters informed by a detailed COMSOL Multiphysics® model, has led to reductions in replication errors in the mirrors. Mandrel surface fabrication was improved by implementing a computer-controlled polishing process that corrected the low-frequency mandrel figure error and achieved <2.0 nm RMS convergence error. X-ray tests performed on a pair of mirror shells replicated from the mandrel have demonstrated <10 µm full-width at half-maximum (FWHM) spatial resolution. Here, we discuss the development process, highlight results from metrology and x-ray testing, and define a path for achieving a program goal of 5 µm FWHM resolution.
ABSTRACT
NASA's Marshall Space Flight Center (MSFC) maintains an active research program toward the development of high-resolution, lightweight, grazing-incidence x-ray optics to serve the needs of future x-ray astronomy missions such as Lynx. MSFC development efforts include both direct fabrication (diamond turning and deterministic computer-controlled polishing) of mirror shells and replication of mirror shells (from figured, polished mandrels). Both techniques produce full-circumference monolithic (primary + secondary) shells that share the advantages of inherent stability, ease of assembly, and low production cost. However, to achieve high-angular resolution, MSFC is exploring significant technology advances needed to control sources of figure error including fabrication- and coating-induced stresses and mounting-induced distortions.
ABSTRACT
The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins, but the molecular details of their activity are not understood. As a first step in the structural characterisation of these proteins, we have analysed their secondary structure and resolved the surface topology of a tetrameric complex of the Vip3Ag4 protein by transmission electron microscopy. Sites sensitive to proteolysis by trypsin are identified and the trypsin-cleaved protein appears to retain a similar structure as an octomeric complex comprising four copies each of the ~65 kDa and ~21 kDa products of proteolysis. This processed form of the toxin may represent the active toxin. The quality and monodispersity of the protein produced in this study make Vip3Ag4 a candidate for more detailed structural analysis using cryo-electron microscopy.
