Properties of multilayer filters Interim report, 1 Sep. 1969 - 28 Feb. 1970

Using films of gold and silver for optical filter

Properties of multilayer filters Interim report, 1 Mar. - 31 Aug. 1969

Blocking filter effects on long-wavelength rejection of ultraviolet bandpass filte

Properties of multilayer filters Final report, 1 Mar. 1964 - 28 Feb. 1967

Optical interference bandpass filters for ultraviolet spectral regio

Properties of Multilayer Filters Interim Report, 1 Sep. 1965 - 28 Feb. 1966

Circuitry and calibration of solenoid actuated shutter for rapid firing of aluminum and design of ultraviolet band pass filte

Grating-coupled excitation of multiple surface plasmon-polariton waves

The excitation of multiple surface-plasmon-polariton (SPP) waves of different linear polarization states and phase speeds by a surface-relief grating formed by a metal and a rugate filter, both of finite thickness, was studied theoretically, using rigorous coupled-wave-analysis. The incident plane wave can be either p or s polarized. The excitation of SPP waves is indicated by the presence of those peaks in the plots of absorbance vs. the incidence angle that are independent of the thickness of the rugate filter. The absorbance peaks representing the excitation of s-polarized SPP waves are narrower than those representing p-polarized SPP waves. Two incident plane waves propagating in different directions may excite the same SPP wave. A line source could excite several SPP waves simultaneously

Structure of the 26S proteasome with ATP-gamma S bound provides insights into the mechanism of nucleotide-dependent substrate translocation

The 26S proteasome is a 2.5-MDa, ATP-dependent multisubunit proteolytic complex that processively destroys proteins carrying a degradation signal. The proteasomal ATPase heterohexamer is a key module of the 19S regulatory particle; it unfolds substrates and translocates them into the 20S core particle where degradation takes place. We used cryoelectron microscopy single-particle analysis to obtain insights into the structural changes of 26S proteasome upon the binding and hydrolysis of ATP. The ATPase ring adopts at least two distinct helical staircase conformations dependent on the nucleotide state. The transition from the conformation observed in the presence of ATP to the predominant conformation in the presence of ATP-gamma S induces a sliding motion of the ATPase ring over the 20S core particle ring leading to an alignment of the translocation channels of the ATPase and the core particle gate, a conformational state likely to facilitate substrate translocation. Two types of inter-subunit modules formed by the large ATPase domain of one ATPase subunit and the small ATPase domain of its neighbor exist. They resemble the contacts observed in the crystal structures of ClpX and proteasome-activating nucleotidase, respectively. The ClpX-like contacts are positioned consecutively and give rise to helical shape in the hexamer, whereas the proteasome-activating nucleotidase-like contact is required to close the ring. Conformational switching between these forms allows adopting different helical conformations in different nucleotide states. We postulate that ATP hydrolysis by the regulatory particle ATPase (Rpt) 5 subunit initiates a cascade of conformational changes, leading to pulling of the substrate, which is primarily executed by Rpt1, Rpt2, and Rpt6

Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome

The 26S proteasome is a 2.5 MDa molecular machine that executes the degradation of substrates of the ubiquitin-proteasome pathway. The molecular architecture of the 26S proteasome was recently established by cryo-EM approaches. For a detailed understanding of the sequence of events from the initial binding of polyubiquitylated substrates to the translocation into the proteolytic core complex, it is necessary to move beyond static structures and characterize the conformational landscape of the 26S proteasome. To this end we have subjected a large cryo-EM dataset acquired in the presence of ATP and ATP-gamma S to a deep classification procedure, which deconvolutes coexisting conformational states. Highly variable regions, such as the density assigned to the largest subunit, Rpn1, are now well resolved and rendered interpretable. Our analysis reveals the existence of three major conformations: in addition to the previously described ATP-hydrolyzing (ATP(h)) and ATP-gamma S conformations, an intermediate state has been found. Its AAA-ATPase module adopts essentially the same topology that is observed in the ATP(h) conformation, whereas the lid is more similar to the ATP-gamma S bound state. Based on the conformational ensemble of the 26S proteasome in solution, we propose a mechanistic model for substrate recognition, commitment, deubiquitylation, and translocation into the core particle