Laue diffraction lenses for astrophysics: Theoretical concepts
نویسندگان
چکیده
منابع مشابه
MAX: Development of a Laue diffraction lens for nuclear astrophysics
The next generation of instrumentation for nuclear astrophysics will have to achieve an improvement in sensitivity by a factor of 10-100 over present technologies. With the focusing gammaray telescope MAX we take up this challenge and propose to combine the required sensitivity with high spectral and angular resolution, and the capability to measure the polarization of the photons. MAX is a spa...
متن کاملFocusing with multilayer Laue lenses
1DESY, Notkestr. 85, 22607 Hamburg, Germany, 2CFEL at DESY, Notkestr. 85, 22607 Hamburg, Germany, 3Institute of Experimental Physics, University of Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany, 4SLAC National Accelerator Laboratory, 2575 Sand Hill Road MS 29, Menlo Park, CA 94025, USA, 5Faculty of Physics, University of Bialystok, ul. Lipowa 41, 15-424 Bialystok, Poland, 6European XFEL...
متن کاملHigh numerical aperture multilayer Laue lenses
The ever-increasing brightness of synchrotron radiation sources demands improved X-ray optics to utilise their capability for imaging and probing biological cells, nanodevices, and functional matter on the nanometer scale with chemical sensitivity. Here we demonstrate focusing a hard X-ray beam to an 8 nm focus using a volume zone plate (also referred to as a wedged multilayer Laue lens). This ...
متن کاملTime-resolved Laue diffraction of deforming micropillars.
We demonstrate real-time resolved white beam Laue diffraction during compression of micron-sized focused ion beam milled single crystals Au pillars, revealing the dynamical correlation between microstructure and plasticity. The evolution of the Laue patterns of the Au pillars demonstrates the occurrence of crystal rotation and strengthening is explained by plasticity starting on a slip system t...
متن کاملStatic Laue diffraction studies on acetylcholinesterase.
Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to, and products from, the active site, which may be investigated by time-resolved crystallography. In order to address one aspect of the feasibility ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Experimental Astronomy
سال: 2006
ISSN: 0922-6435,1572-9508
DOI: 10.1007/s10686-006-9064-z