Electron diffraction of helical structures

1992 ◽  
Vol 50 (1) ◽  
pp. 518-519
Author(s):  
T. Ruiz ◽  
R. Diaz ◽  
J-L. Ranck ◽  
D.L.D. Caspar ◽  
D.J. DeRosier
Keyword(s):  
Electron Microscopy ◽  
Electron Diffraction ◽  
Helical Structure ◽  
Lipid Monolayer ◽  
Electron Diffraction Data ◽  
Helical Structures ◽  
Protein Aggregate ◽  
X Ray ◽  
Isomorphous Replacement ◽  
Diffraction Patterns

Electron microscopy has advantages over X-ray diffraction for the study of helical structures. For X-ray studies, one needs large well oriented samples which are difficult to obtain. Only one helical structure, TMV, has been solved by conventional X-ray analysis using multiple isomorphous replacement. In contrast, one requires single particles or small rafts for studies by electron microscopy. We are attempting to use a combination of imaging and electron diffraction data to analyze helical structures at 9-10 Å resolution in order to visualize α-helices. To obtain electron diffraction patterns we produced well-ordered domains (∽ 1-3 μm in diameter) for diffraction work. Several methods succeeded in aligning helical particles : the lipid monolayer technique, mica sandwiching and unidirectional blotting. The lipid monolayer technique proved to be the best for high resolution work. The three samples under study (flagellar filaments from Salmonella typhimurium, TMV and TMV stacked disk protein aggregate) gave electron diffraction patterns out to ∽10 Å resolution.

Dynamical Scattering in Electron Diffraction of wet Protein Crystals

1980 ◽  
Vol 38 ◽  
pp. 42-43
Author(s):  
B. B. Chang ◽  
D. F. Parsons
Keyword(s):  
Electron Diffraction ◽  
Scattering Theory ◽  
Protein Crystals ◽  
Electron Diffraction Data ◽  
Specimen Thickness ◽  
Major Question ◽  
X Ray ◽  
Scattering Effects ◽  
Diffraction Patterns ◽  
Acceleration Voltage

The significance of dynamical scattering effects remains the major question in the structural analysis by electron diffraction of protein crystals preserved in the hydrated state. In the few cases (single layers of purple membrane and 400-600 Å thick catalase crystals examined at 100 kV acceleration voltage) where electron-diffraction patterns were used quantitatively, dynamical scattering effects were considered unimportant on the basis of a comparison with x-ray intensities. The kinematical treatment is usually justified by the thinness of the crystal. A theoretical investigation by Ho et al. using Cowley-Moodie multislice formulation of dynamical scattering theory and cytochrome b5as the test object2 suggests that kinematical analysis of electron diffraction data with 100-keV electrons would not likely be valid for specimen thickness of 300 Å or more. We have chosen to work with electron diffraction patterns obtained from actual wet protein crystals (rat hemoglobin crystals of thickness range 1000 to 2500 Å) at 200 and 1000 kV and to analyze these for dynamical effects.

Atomic structure of YB56 studied by digital high-resolution electron microscopy and electron diffraction

2001 ◽  
Vol 16 (1) ◽  
pp. 101-107 ◽  
Author(s):  
Takeo Oku ◽  
Jan-Olov Bovin ◽  
Iwami Higashi ◽  
Takaho Tanaka ◽  
Yoshio Ishizawa
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Electron Diffraction ◽  
High Resolution Electron Microscopy ◽  
Charge Coupled Device ◽  
X Ray ◽  
Resolution Electron ◽  
High Resolution Images ◽  
Diffraction Patterns ◽  
Simulated Images

Atomic positions for Y atoms were determined by using high-resolution electron microscopy and electron diffraction. A slow-scan charge-coupled device camera which had high linearity and electron sensitivity was used to record high-resolution images and electron diffraction patterns digitally. Crystallographic image processing was applied for image analysis, which provided more accurate, averaged Y atom positions. In addition, atomic disordering positions in YB56 were detected from the differential images between observed and simulated images based on x-ray data, which were B24 clusters around the Y-holes. The present work indicates that the structure analysis combined with digital high-resolution electron microscopy, electron diffraction, and differential images is useful for the evaluation of atomic positions and disordering in the boron-based crystals.

Halloysite in some soils from north-east Scotland

Clay Minerals ◽  
1977 ◽  
Vol 12 (1) ◽  
pp. 59-66 ◽  
Author(s):  
M. J. Wilson ◽  
J. M. Tait
Keyword(s):  
Electron Microscopy ◽  
Electron Diffraction ◽  
Soil Samples ◽  
X Ray Diffraction ◽  
X Ray ◽  
Drainage Class ◽  
North East ◽  
Parent Rocks ◽  
Diffraction Patterns

AbstractX-ray diffraction and electron microscopy show that halloysite occurs widely in soils derived from a variety of parent rocks (granite, gabbro, schist and slate) in north-east Scotland. Both tubular and non-tubular forms are observed, the latter being characterized by electron diffraction patterns with 001 reflection either absent or very weak and diffuse. Clay fractions from a poorly drained profile separated without prior drying of the soil samples contain essentially dehydrated halloysite at the surface, this becoming progressively more hydrated with depth. Since halloysite occurs extensively in soils of widely varying drainage class the mineral is probably not the result of recent soilforming processes but may have originated during Tertiary or interglacial weathering.

A complex pseudo-decagonal quasicrystal approximant, Al37(Co,Ni)15.5, solved by rotation electron diffraction

2014 ◽  
Vol 47 (1) ◽  
pp. 215-221 ◽  
Author(s):  
Devinder Singh ◽  
Yifeng Yun ◽  
Wei Wan ◽  
Benjamin Grushko ◽  
Xiaodong Zou ◽  
...  
Keyword(s):  
Electron Diffraction ◽  
Single Crystal ◽  
Diffraction Data ◽  
Three Dimensional ◽  
Basic Structure ◽  
Electron Diffraction Data ◽  
Dimensional Electron ◽  
X Ray Diffraction ◽  
X Ray ◽  
Diffraction Patterns

Electron diffraction is a complementary technique to single-crystal X-ray diffraction and powder X-ray diffraction for structure solution of unknown crystals. Crystals too small to be studied by single-crystal X-ray diffraction or too complex to be solved by powder X-ray diffraction can be studied by electron diffraction. The main drawbacks of electron diffraction have been the difficulties in collecting complete three-dimensional electron diffraction data by conventional electron diffraction methods and the very time-consuming data collection. In addition, the intensities of electron diffraction suffer from dynamical scattering. Recently, a new electron diffraction method, rotation electron diffraction (RED), was developed, which can overcome the drawbacks and reduce dynamical effects. A complete three-dimensional electron diffraction data set can be collected from a sub-micrometre-sized single crystal in less than 2 h. Here the RED method is applied forab initiostructure determination of an unknown complex intermetallic phase, the pseudo-decagonal (PD) quasicrystal approximant Al37.0(Co,Ni)15.5, denoted as PD2. RED shows that the crystal is F-centered, witha= 46.4,b= 64.6,c= 8.2 Å. However, as with other approximants in the PD series, the reflections with oddlindices are much weaker than those withleven, so it was decided to first solve the PD2 structure in the smaller, primitive unit cell. The basic structure of PD2 with unit-cell parametersa= 23.2,b= 32.3,c= 4.1 Å and space groupPnmmhas been solved in the present study. The structure withc= 8.2 Å will be taken up in the near future. The basic structure contains 55 unique atoms (17 Co/Ni and 38 Al) and is one of the most complex structures solved by electron diffraction. PD2 is built of characteristic 2 nm wheel clusters with fivefold rotational symmetry, which agrees with results from high-resolution electron microscopy images. Simulated electron diffraction patterns for the structure model are in good agreement with the experimental electron diffraction patterns obtained by RED.

Electron-diffraction patterns from frozen hydrate protein microcrystals: A new tool instructural studies

1994 ◽  
Vol 52 ◽  
pp. 102-103
Author(s):  
Christoph Burmester ◽  
Kenneth C. Holmes ◽  
Rasmus R. Schröder
Keyword(s):  
Electron Diffraction ◽  
Diffraction Data ◽  
Heavy Atom ◽  
Atomic Resolution ◽  
Protein Crystals ◽  
Electron Diffraction Data ◽  
Phase Information ◽  
Isomorphous Replacement ◽  
Diffraction Patterns

Electron crystallography of 2D protein crystals can yield models with atomic resolution by taking Fourier amplitudes from electron diffraction and phase information from processed images. Imaging at atomic resolution is more difficult than the recording of corresponding electron diffraction patterns. Therefore attempts have been made to recover phase information from diffraction data from 2-D and 3-D crystals by the method of isomorphous replacement using heavy atom labelled protein crystals. These experiments, however, have so far not produced usable phase information, partly because of the large experimental error in the spot intensities. Here we present electron diffraction data obtained from frozen hydrated 3-D protein crystals with an energy-filter microscope and a specially constructed Image Plate scanner which are of considerably better crystallographic quality (as evidenced in much smaller values for the crystallographic R-factors Rsym and Rmerge) than those reported before. The quality of this data shows that the method of isomorphous replacement could indeed be used for phase determination for diffraction data obtained from 3-D microcrystals by electron diffraction.

Accurate Recording and Measurement of Electron Diffraction Data in Structural and Difference Fourier Studies of Proteins

2001 ◽  
Vol 7 (5) ◽  
pp. 407-417
Author(s):  
Kenneth H. Downing ◽  
Huilin Li
Keyword(s):  
Electron Diffraction ◽  
Diffraction Data ◽  
Drug Binding ◽  
Electron Diffraction Data ◽  
Mathematical Basis ◽  
X Ray ◽  
X Ray Crystallography ◽  
High Resolution Images ◽  
Diffraction Patterns ◽  
Difference Fourier

AbstractMany of the techniques that have been developed in X-ray crystallography are being applied in electron crystallographic studies of proteins. Electron crystallography has the advantage of measuring structure factor phases directly from high resolution images with an accuracy substantially higher than is common in X-ray crystallography. However, electron diffraction amplitudes are often not as precise as those obtained in X-ray work. We discuss here some approaches to maximizing the reliability of the diffraction amplitudes through choice of exposure and data processing schemes. With accurate measurement of diffraction data, Fourier difference methods can be used in electron crystallographic studies of small, localized changes of proteins that exist in two-dimensional crystals. The mathematical basis for the power of these methods in detecting small changes is reviewed. We then discuss several issues related to optimizing the quality of the diffraction data and derive an expression for the best exposure for recording diffraction patterns. An application of Fourier difference maps in localizing drug binding sites on the protein tubulin is discussed.

Multiple isomorphous replacement for phase determination in protein crystals

1995 ◽  
Vol 53 ◽  
pp. 856-857
Author(s):  
Christoph Burmester ◽  
Kenneth C. Holmes ◽  
Rasmus R. Schröder
Keyword(s):  
Electron Diffraction ◽  
Heavy Atom ◽  
Atomic Resolution ◽  
Protein Crystals ◽  
Electron Diffraction Data ◽  
Phase Information ◽  
Electron Dose ◽  
Isomorphous Replacement ◽  
Resolution Electron ◽  
Diffraction Patterns

Electron crystallography of 2D protein crystals can yield models with atomic resolution by taking Fourier amplitudes from electron diffraction and phase information from processed images. Imaging at atomic resolution is more difficult than the recording of corresponding high resolution electron diffraction patterns. Therefore attempts have been made to retrieve phase information from diffraction from heavy atom labelled protein crystals. The expected differences between native and labelled crystals are small, therefore a high experimental accuracy is necessary. This is achieved by the use of energy filter TEM and image plates, as dicussed in. Here we present electron diffraction data obtained from frozen hydrated 3D protein crystals with an energy filter microspcope and a specially designed image plate scanner. Data were recorded for the native crystal as well as for two different heavy atom derivatives. Differences between the native and the derivate forms can be detected and are significant.Electron diffraction patterns from frozen hydrated catalase crystals were recorded on an EFTEM Zeiss 912 Ω (120kV, zero loss mode, energy width ΔE=10eV, electron dose 5 e-/A2) using image plates and a quasi confocal scanner readout.

scholarly journals Reconstructing three-dimensional helical structure with an X-ray free electron laser

2016 ◽  
Vol 49 (2) ◽  
pp. 450-456
Author(s):  
M. Uddin
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
National Laboratory ◽  
Three Dimensional ◽  
Helical Structure ◽  
Dimensional Structure ◽  
Helical Structures ◽  
X Ray ◽  
Research Priority ◽  
Diffraction Patterns

Recovery of three-dimensional structure from single-particle X-ray scattering of completely randomly oriented diffraction patterns as predicted a few decades ago has been realized owing to the advent of the new emerging X-ray free electron laser (XFEL) technology. Since the world's first XFEL started operation in June 2009 at SLAC National Laboratory at Stanford, the first few experiments have been conducted on larger objects such as viruses. Many of the important structures of nature such as helical viruses or DNA consist of helical repetition of biological subunits. Hence development of a method for reconstructing helical structure from collected XFEL data has been a top research priority. This work describes the development of a method for solving helical structures such as tobacco mosaic virus from a set of randomly oriented simulated diffraction patterns exploiting the symmetry and Fourier space constraint of the diffraction volume.

Identification of a new trace 114R SiC by HREM

1999 ◽  
Vol 55 (2) ◽  
pp. 255-257 ◽  
Author(s):  
X. Y. Yang ◽  
G. Y. Shi ◽  
X. M. Meng ◽  
H. L. Huang ◽  
Y. K. Wu
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Electron Diffraction ◽  
Matrix Model ◽  
High Resolution Electron Microscopy ◽  
Stacking Sequence ◽  
X Ray Diffraction ◽  
X Ray ◽  
Resolution Electron ◽  
Diffraction Patterns

Using electron diffraction patterns and high-resolution electron microscopy (HREM), a trace 114R SiC in commercial α-SiC powder (mainly 6H SiC according to X-ray diffraction) has been discovered. In a hexagonal unit cell its stacking sequence is [(33)4(34)2]3, the periodicity along the c axis is 286.14 Å and a = b = 3.073 Å. 114R belongs to the structure series of (33) n34(33) m34 predicted theoretically by Pandey & Krishna [Mater. Sci. Eng. (1975), 20, 243–249] on the basis of the faulted matrix model.

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.

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