Structure factors and phonon dispersion in liquid Li0.61Na0.39 alloy

Pramana ◽  
2004 ◽  
Vol 63 (2) ◽  
pp. 431-435 ◽  
Author(s):  
Arun Pratap ◽  
Kirit N. Lad ◽  
K. G. Raval
Keyword(s):  
Phonon Dispersion ◽  
Structure Factors

Some Applications of the U. S. Steel MVEM

1973 ◽  
Vol 31 ◽  
pp. 4-5
Author(s):  
J. S. Lally ◽  
L. E. Thomas ◽  
R. M. Fisher
Keyword(s):  
Electron Diffraction ◽  
Debye Temperature ◽  
Metals And Alloys ◽  
Critical Voltage ◽  
Dynamical Diffraction ◽  
Phase Structures ◽  
Structure Factors ◽  
Local Bonding ◽  
Diffraction Phenomenon ◽  
Multi Phase

A variety of materials containing many different microstructures have been examined with the USS MVEM. Three topics have been selected to illustrate some of the more recent studies of diffraction phenomena and defect, grain and multi-phase structures of metals and minerals.(1) Critical Voltage Effects in Metals and Alloys - This many-beam dynamical diffraction phenomenon, in which some Bragg resonances vanish at certain accelerating voltages, Vc, depends sensitively on the spacing of diffracting planes, Debye temperature θD and structure factors. Vc values can be measured to ± 0.5% in the HVEM ana used to obtain improved extinction distances and θD values appropriate to electron diffraction, as well as to probe local bonding effects and composition variations in alloys.

Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

1983 ◽  
Vol 41 ◽  
pp. 446-447
Author(s):  
William F. Tivol ◽  
Murray Vernon King ◽  
D. F. Parsons
Keyword(s):  
Electron Diffraction ◽  
Heavy Atom ◽  
Isomorphous Substitution ◽  
X Ray Diffraction ◽  
Salt Solutions ◽  
X Ray ◽  
Isomorphous Replacement ◽  
Structure Factors ◽  
Diffraction Structure ◽  
The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

Sign in / Sign up

Export Citation Format

Share Document