Future needs in Army structures, structural dynamics, and materials research

1988 ◽  
Author(s):  
G. MAYER
Author(s):  
Charles W. Allen

High voltage TEMs were introduced commercially thirty years ago, with the installations of 500 kV Hitachi instruments at the Universities of Nogoya and Tokyo. Since that time a total of 51 commercial instruments, having maximum accelerating potentials of 0.5-3.5 MV, have been delivered. Prices have gone from about a dollar per volt for the early instruments to roughly twenty dollars per volt today, which is not so unreasonable considerinp inflation and vastly improved electronics and other improvements. The most expensive HVEM (the 3.5 MV instrument at Osaka University) cost about 5 percent of the construction cost of the USA's latest synchrotron.Table 1 briefly traces the development of HVEM in this country for the materials sciences. There are now only three available instruments at two sites: the 1.2 MeV HVEM at Argonne National Lab, and 1.0 and 1.5 MeV instruments at Lawrence Berkeley National Lab. Fortunately, both sites are user facilities funded by DOE for the materials research community.


2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.


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