Crystal-bending and high-resolution protein-structure determination from electron-diffraction data

1977 ◽  
Vol 64 (12) ◽  
pp. 637-638 ◽  
Author(s):  
D. L. Dorset ◽  
Sek -Wen Hui
Keyword(s):  
Protein Structure ◽  
High Resolution ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Protein Structure Determination ◽  
Electron Diffraction Data

Crystal Structure Determination of Glycerol-Containing Lipids from Electron Diffraction Data. Use of Analog Compounds Based upon Configurational Isomers of Cyclopentane-1, 2, 3-TRIOL

1977 ◽  
Vol 35 ◽  
pp. 24-25
Author(s):  
Douglas L. Dorset ◽  
Anthony J. Hancock
Keyword(s):  
Crystal Structure ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Crystal Surface ◽  
Coherent Scattering ◽  
Crystal Structure Determination ◽  
Electron Diffraction Data ◽  
Polar Group ◽  
Axis Orientation

Lipids containing long polymethylene chains were among the first compounds subjected to electron diffraction structure analysis. It was only recently realized, however, that various distortions of thin lipid microcrystal plates, e.g. bends, polar group and methyl end plane disorders, etc. (1-3), restrict coherent scattering to the methylene subcell alone, particularly if undistorted molecular layers have well-defined end planes. Thus, ab initio crystal structure determination on a given single uncharacterized natural lipid using electron diffraction data can only hope to identify the subcell packing and the chain axis orientation with respect to the crystal surface. In lipids based on glycerol, for example, conformations of long chains and polar groups about the C-C bonds of this moiety still would remain unknown.One possible means of surmounting this difficulty is to investigate structural analogs of the material of interest in conjunction with the natural compound itself. Suitable analogs to the glycerol lipids are compounds based on the three configurational isomers of cyclopentane-1,2,3-triol shown in Fig. 1, in which three rotameric forms of the natural glycerol derivatives are fixed by the ring structure (4-7).

scholarly journals Procedure and Computer Programs for the Structure Determination of Gaseous Molecules from Electron Diffraction Data.

1969 ◽  
Vol 23 ◽  
pp. 3224-3234 ◽  
Author(s):  
B. Andersen ◽  
H. M. Seip ◽  
T. G. Strand ◽  
R. Stølevik ◽  
Gunner Borch ◽  
...  
Keyword(s):  
Electron Diffraction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Computer Programs ◽  
Electron Diffraction Data

STRUCTURE DETERMINATION OF THE Ge(111)-(3×1)Ag SURFACE RECONSTRUCTION

1999 ◽  
Vol 06 (06) ◽  
pp. 1061-1065 ◽  
Author(s):  
D. GROZEA ◽  
E. BENGU ◽  
C. COLLAZO-DAVILA ◽  
L. D. MARKS
Keyword(s):  
Electron Diffraction ◽  
Surface Reconstruction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Heavy Atom ◽  
Direct Methods ◽  
Electron Diffraction Data ◽  
Transmission Electron ◽  
First Time

For the first time, during the investigation of the Ag submonolayer on the Ge(111) system, large, independent domains of the Ge (111)-(3×1) Ag phase were imaged and investigated. Previous studies have reported it only as small insets between Ge (111)-(4×4) Ag and Ge (111)- c (2×8) domains. The transmission electron diffraction data were analyzed using a Direct Methods approach and "heavy-atom holography," with the result of an atomic model of the structure similar to that of Ge (111)-(3×1) Ag .

scholarly journals De Novo High-Resolution Protein Structure Determination from Sparse Spin-Labeling EPR Data

Structure ◽  
2008 ◽  
Vol 16 (2) ◽  
pp. 181-195 ◽  
Author(s):  
Nathan Alexander ◽  
Ahmad Al-Mestarihi ◽  
Marco Bortolus ◽  
Hassane Mchaourab ◽  
Jens Meiler
Keyword(s):  
Protein Structure ◽  
High Resolution ◽  
Structure Determination ◽  
De Novo ◽  
Protein Structure Determination ◽  
Spin Labeling

Effect of diffraction crystallography on HREM

2003 ◽  
Vol 218 (4) ◽  
Author(s):  
Fang-hua Li
Keyword(s):  
Image Processing ◽  
High Resolution ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Heavy Atom ◽  
Empirical Method ◽  
Crystal Defects ◽  
Electron Diffraction Data ◽  
Crystal Thickness ◽  
Resolution Electron

AbstractA simple image contrast theory in high-resolution electron microscopy (HREM) is introduced to demonstrate that below a certain critical crystal thickness the intensity of the Scherzer focus image is linear to the projected potential of an artificial crystal that is isomorphic to the examined one. It has become the theoretical base of electron crystallographic image processing techniques relying on the weak-phase-object approximation and kinematical diffraction. Two techniques of image processing are introduced. One of them aims at determining crystal structures by combining electron diffraction data and applying diffraction analysis methods. To reduce various kinds of electron diffraction intensity distortion the diffraction data are corrected by means of an empirical method set up by referring to the heavy atom method and Wilson statistic. The other one aims at revealing crystal defects at atomic resolution from the image taken with a medium-voltage field-emission high-resolution electron microscope. The dynamical effect is corrected by forcing the integral amplitudes of reflections in the diffractogram of image equal to the amplitudes of corresponding structure factors for the perfect crystal. The principle of the two techniques is briefly introduced, and examples of applications to crystal structure and defect determination are given.

scholarly journals Gently does it for submicron crystals

eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Oliver B Zeldin ◽  
Axel T Brunger
Keyword(s):  
Electron Beam ◽  
Protein Structure ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Three Dimensional ◽  
Electron Diffraction Data ◽  
Large Numbers ◽  
Diffraction Patterns ◽  
Weak Electron

A protein structure has been refined with electron diffraction data obtained by using a very weak electron beam to collect large numbers of diffraction patterns from a few sub-micron-sized three-dimensional crystals.

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