Effects of Electron Correlation in X-Ray and Electron Diffraction

In the investigation of the molecular organization of cell membranes it is often supposed that lipid molecules are arranged in a bimolecular film. X-ray diffraction data obtained in a direction perpendicular to the plane of suitably layered membrane systems have generally been interpreted in accord with such a model of the membrane structure. The present studies were begun in order to determine whether selected area electron diffraction would provide a tool of sufficient sensitivity to permit investigation of the degree of intermolecular order within lipid films. The ultimate objective would then be to apply the method to single fragments of cell membrane material in order to obtain data complementary to the transverse data obtainable by x-ray diffraction.

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Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100075968 ◽

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.

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The structure of amorphous and polycrystalline materials using energy-filtered RDF analysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100130584 ◽

1992 ◽

Vol 50 (2) ◽

pp. 1190-1191

Author(s):

David Cockayne ◽

David McKenzie

Keyword(s):

Electron Diffraction ◽

Diffraction Pattern ◽

Density Function ◽

Electron Diffraction Pattern ◽

Polycrystalline Materials ◽

Nearest Neighbour ◽

X Ray ◽

Selected Area Electron Diffraction ◽

Reduced Density ◽

System F

The technique of Electron Reduced Density Function (RDF) analysis has ben developed into a rapid analytical tool for the analysis of small volumes of amorphous or polycrystalline materials. The energy filtered electron diffraction pattern is collected to high scattering angles (currendy to s = 2 sinθ/λ = 6.5 Å-1) by scanning the selected area electron diffraction pattern across the entrance aperture to a GATAN parallel energy loss spectrometer. The diffraction pattern is then converted to a reduced density function, G(r), using mathematical procedures equivalent to those used in X-ray and neutron diffraction studies.Nearest neighbour distances accurate to 0.01 Å are obtained routinely, and bond distortions of molecules can be determined from the ratio of first to second nearest neighbour distances. The accuracy of coordination number determinations from polycrystalline monatomic materials (eg Pt) is high (5%). In amorphous systems (eg carbon, silicon) it is reasonable (10%), but in multi-element systems there are a number of problems to be overcome; to reduce the diffraction pattern to G(r), the approximation must be made that for all elements i,j in the system, fj(s) = Kji fi,(s) where Kji is independent of s.

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