scholarly journals Two-dimensional crystals formed from photosynthetic reaction centers.

1983 ◽  
Vol 97 (4) ◽  
pp. 1266-1270 ◽  
Author(s):  
K R Miller ◽  
J S Jacob
Keyword(s):  
Electron Microscopy ◽  
Single Unit ◽  
Reaction Centers ◽  
Unit Cell ◽  
Two Dimensional ◽  
Photosynthetic Reaction Centers ◽  
Photosynthetic Membranes ◽  
Fourier Techniques ◽  
High Degree ◽  
Degree Of Order

Photosynthetic reaction centers from the bacterium Rhodopseudomonas viridis were prepared after detergent solubilization of photosynthetic membranes. The purified reaction centers, in agreement with reports from other laboratories, contain four distinct polypeptides ranging in molecular weight from 28,000 to 41,000. When the detergent was gradually removed by dialysis under appropriate conditions, large two-dimensional sheets of reaction centers were formed, suitable for analysis by electron microscopy. The crystals were rectangular, and the dimensions of a single unit cell were 121 X 129 A. Each unit cell contained four distinct subunits, each with approximate dimensions of 45 X 60 A. The thickness of the sheet was 60 A. Preliminary studies of the sheets with negative staining indicated that the sheets show a high degree of order: as many as six orders are visible in transforms of the images. Because of the fact that in R. viridis the native membrane from which these reaction centers were purified also displays a crystal-like structure, comparative studies between a membrane and one of its components, each analyzed by Fourier techniques, are now possible.

scholarly journals Two-Dimensional Zeolite Materials: Structural and Acidity Properties

Materials ◽  
2020 ◽  
Vol 13 (8) ◽  
pp. 1822 ◽  
Author(s):  
Emily Schulman ◽  
Wei Wu ◽  
Dongxia Liu
Keyword(s):  
Single Unit ◽  
Active Sites ◽  
Three Dimensional ◽  
Total Surface Area ◽  
Unit Cell ◽  
Future Research ◽  
Two Dimensional ◽  
Beneficial Effects ◽  
Surface Areas ◽  
Composition Properties

Zeolites are generally defined as three-dimensional (3D) crystalline microporous aluminosilicates in which silicon (Si4+) and aluminum (Al3+) are coordinated tetrahedrally with oxygen to form large negative lattices and consequent Brønsted acidity. Two-dimensional (2D) zeolite nanosheets with single-unit-cell or near single-unit-cell thickness (~2–3 nm) represent an emerging type of zeolite material. The extremely thin slices of crystals in 2D zeolites produce high external surface areas (up to 50% of total surface area compared to ~2% in micron-sized 3D zeolite) and expose most of their active sites on external surfaces, enabling beneficial effects for the adsorption and reaction performance for processing bulky molecules. This review summarizes the structural properties of 2D layered precursors and 2D zeolite derivatives, as well as the acidity properties of 2D zeolite derivative structures, especially in connection to their 3D conventional zeolite analogues’ structural and compositional properties. The timeline of the synthesis and recognition of 2D zeolites, as well as the structure and composition properties of each 2D zeolite, are discussed initially. The qualitative and quantitative measurements on the acid site type, strength, and accessibility of 2D zeolites are then presented. Future research and development directions to advance understanding of 2D zeolite materials are also discussed.

Correlation averaging: Lattice separation and resolution assessment

1986 ◽  
Vol 44 ◽  
pp. 140-143
Author(s):  
M. Radermacher ◽  
J. Frank ◽  
C.A. Mannella
Keyword(s):  
Electron Microscopy ◽  
Single Layer ◽  
Theoretical Background ◽  
Unit Cell ◽  
Two Dimensional ◽  
Established Technique

Correlation averaging is a well established technique and has been extensively applied to the analysis of two-dimensional arrays in electron microscopy. The resolution of the structure of the unit cell can be improved in many situations compared to the resolution achievable by Fourier filtration techniques. Lattices of a specimen consisting of more than a single layer array can be reconstructed separately. we have analysed the theoretical background of some of the steps involved in the procedure. Our results confirm that a separate reconstruction of single overlapped layers is possible whenever the conditions found necessary for lattice separation by Fourier filtration are met.

scholarly journals Two-dimensional crystals of photosystem II: biochemical characterization, cryoelectron microscopy and localization of the D1 and cytochrome b559 polypeptides.

1996 ◽  
Vol 132 (5) ◽  
pp. 823-833 ◽  
Author(s):  
K M Marr ◽  
D N Mastronarde ◽  
M K Lyon
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Biochemical Characterization ◽  
Higher Plants ◽  
Unit Cell ◽  
Two Dimensional ◽  
Cytochrome B559 ◽  
Ps Ii

Photosystem II (PS II) is a photosynthetic reaction center found in higher plants which has the unique ability to evolve oxygen from water. Several groups have formed two-dimensional PS II crystals or have isolated PS II complexes and studied them by electron microscopy and image analysis. The majority of these specimens have not been well characterized biochemically and have yielded relatively low resolution two-dimensional projection maps with a variety of unit cell sizes. We report the characterization of the polypeptide and lipid content of tubular crystals of PS II. The crystals contain the reaction center core polypeptides D1, D2, cytochrome b559, as well as the chlorophyll-binding polypeptides (CP) CP47, CP43, CP29, CP26, CP24, and CP22. The lipid composition was similar to the lipids found in the stacked portion of thylakoids. We also report a 2.0-nm resolution projection map determined by electron microscopy and image analysis of frozen, hydrated PS II crystals. This projection map includes information on the portion of the complex buried in the lipid bilayer. The unit cell is a dimer with unit vectors of 17.0 and 11.4 nm separated by an angle of 106.6 degrees. In addition, Fab fragments against D1 and cytochrome b559 were used to localize those two polypeptides, and thus the reaction center, within the PS II complex. The results indicate that D1 and cytochrome b559 are found within one of the heaviest densities of the monomeric unit.

Tissue section lifting for electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 86-87
Author(s):  
Adrian F. van Dellen
Keyword(s):  
Infectious Disease ◽  
Electron Microscopy ◽  
Tissue Culture ◽  
Organ System ◽  
Surrounding Tissue ◽  
Paraffin Sections ◽  
Surface Areas ◽  
Specific Determination ◽  
High Degree ◽  
Accuracy And Repeatability

The morphologic pathologist may require information on the ultrastructure of a non-specific lesion seen under the light microscope before he can make a specific determination. Such lesions, when caused by infectious disease agents, may be sparsely distributed in any organ system. Tissue culture systems, too, may only have widely dispersed foci suitable for ultrastructural study. In these situations, when only a few, small foci in large tissue areas are useful for electron microscopy, it is advantageous to employ a methodology which rapidly selects a single tissue focus that is expected to yield beneficial ultrastructural data from amongst the surrounding tissue. This is in essence what "LIFTING" accomplishes. We have developed LIFTING to a high degree of accuracy and repeatability utilizing the Microlift (Fig 1), and have successfully applied it to tissue culture monolayers, histologic paraffin sections, and tissue blocks with large surface areas that had been initially fixed for either light or electron microscopy.

Electron Microscopy in Molecular Biology

1967 ◽  
Vol 25 ◽  
pp. 2-3
Author(s):  
Cecil E. Hall
Keyword(s):  
Electron Microscopy ◽  
Molecular Biology ◽  
Noise Level ◽  
Molecular Structures ◽  
Material Structure ◽  
The Arts ◽  
Shadow Casting ◽  
Electron Image ◽  
High Degree ◽  
Very High

The visualization of organic macromolecules such as proteins, nucleic acids, viruses and virus components has reached its high degree of effectiveness owing to refinements and reliability of instruments and to the invention of methods for enhancing the structure of these materials within the electron image. The latter techniques have been most important because what can be seen depends upon the molecular and atomic character of the object as modified which is rarely evident in the pristine material. Structure may thus be displayed by the arts of positive and negative staining, shadow casting, replication and other techniques. Enhancement of contrast, which delineates bounds of isolated macromolecules has been effected progressively over the years as illustrated in Figs. 1, 2, 3 and 4 by these methods. We now look to the future wondering what other visions are waiting to be seen. The instrument designers will need to exact from the arts of fabrication the performance that theory has prescribed as well as methods for phase and interference contrast with explorations of the potentialities of very high and very low voltages. Chemistry must play an increasingly important part in future progress by providing specific stain molecules of high visibility, substrates of vanishing “noise” level and means for preservation of molecular structures that usually exist in a solvated condition.

Reconstruction of Two-Dimensional Projections of GP 32*I

1981 ◽  
Vol 39 ◽  
pp. 38-39
Author(s):  
H.A. Cohen ◽  
W. Chiu ◽  
J. Hosoda
Keyword(s):  
Electron Microscopy ◽  
Molecular Weight ◽  
Uranyl Acetate ◽  
Distilled Water ◽  
Acetate Solution ◽  
Two Dimensional ◽  
Parent Molecule ◽  
T4 Bacteriophage ◽  
Electron Imaging ◽  
Better Than

GP 32 (molecular weight 35000) is a T4 bacteriophage protein that destabilizes the DNA helix. The fragment GP32*I (77% of the total weight), which destabilizes helices better than does the parent molecule, crystallizes as platelets thin enough for electron diffraction and electron imaging. In this paper we discuss the structure of this protein as revealed in images reconstructed from stained and unstained crystals.Crystals were prepared as previously described. Crystals for electron microscopy were pelleted from the buffer suspension, washed in distilled water, and resuspended in 1% glucose. Two lambda droplets were placed on grids over freshly evaporated carbon, allowed to sit for five minutes, and then were drained. Stained crystals were prepared the same way, except that prior to draining the droplet, two lambda of aqueous 1% uranyl acetate solution were applied for 20 seconds. Micrographs were produced using less than 2 e/Å2 for unstained crystals or less than 8 e/Å2 for stained crystals.

Feasibility of Molecular Structure Determination With a High Resolution Electron Microscope

1968 ◽  
Vol 26 ◽  
pp. 338-339
Author(s):  
T. A. Welton
Keyword(s):  
Electron Microscope ◽  
Substrate Surface ◽  
Helical Axis ◽  
Base Plane ◽  
Resolution Electron ◽  
High Resolution Electron Microscope ◽  
High Degree ◽  
Degree Of Order ◽  
Purine Pyrimidine

An ultimate design goal for an improved electron microscope, aimed at biological applications, is the determination of the structure of complex bio-molecules. As a prototype of this class of problems, we propose to examine the possibility of reading DNA sequence by an imaginable instrument design. This problem ideally combines absolute importance and relative simplicity, in as much as the problem of enzyme structure seems to be a much more difficult one.The proposed technique involves the deposition on a thin graphite lamina of intact double helical DNA rods. If the structure can be maintained under vacuum conditions, we can then make use of the high degree of order to greatly reduce the work involved in discriminating between the four possible purine-pyrimidine arrangements in each base plane. The phosphorus atoms of the back bone form in projection (the helical axis being necessarily parallel to the substrate surface) two intertwined sinusoids. If these phosphorus atoms have been located up to a certain point on the molecule, we have available excellent information on the orientation of the base plane at that point, and can then locate in projection the key atoms for discrimination of the four alternatives.

Parabolas from Reconstructed Surfaces Observed in Convergent-Beam RHEED Patterns

1990 ◽  
Vol 48 (2) ◽  
pp. 398-399
Author(s):  
M. Gajdardziska-Josifovska
Keyword(s):  
Electron Microscopy ◽  
High Energy ◽  
Two Dimensional ◽  
High Energy Electron ◽  
Reflection And Transmission ◽  
Experimental Diffraction Pattern ◽  
Surface Resonance ◽  
Reconstructed Surfaces ◽  
Reflection Electron Microscopy ◽  
Convergent Beam

Parabolas have been observed in the reflection high-energy electron diffraction (RHEED) patterns from surfaces of single crystals since the early thirties. In the last decade there has been a revival of attempts to elucidate the origin of these surface parabolas. The renewed interest stems from the need to understand the connection between the parabolas and the surface resonance (channeling) condition, the latter being routinely used to obtain higher intensity in reflection electron microscopy (REM) images of surfaces. Several rather diverging descriptions have been proposed to explain the parabolas in the reflection and transmission Kikuchi patterns. Recently we have developed an unifying general treatment in which the parabolas are shown to be K-lines of two-dimensional lattices. Here we want to review the main features of this description and present an experimental diffraction pattern from a 30° MgO (111) surface which displays parabolas that can be attributed to the surface reconstruction.

Two-Dimensional Crystallization of Tetanus Toxin

1985 ◽  
Vol 43 ◽  
pp. 528-529
Author(s):  
Jeffry A. Reidler ◽  
John P. Robinson
Keyword(s):  
Electron Microscopy ◽  
Tetanus Toxin ◽  
Structural Information ◽  
Three Dimensional ◽  
Two Dimensional ◽  
Membrane Interface ◽  
3D Reconstructions ◽  
Cellular Receptors ◽  
Computer Reconstruction ◽  
2D Crystals

We have prepared two-dimensional (2D) crystals of tetanus toxin using procedures developed by Uzgiris and Kornberg for the directed production of 2D crystals of monoclonal antibodies at an antigen-phospholipid monolayer interface. The tetanus toxin crystals were formed using a small mole fraction of the natural receptor, GT1, incorporated into phosphatidyl choline monolayers. The crystals formed at low concentration overnight. Two dimensional crystals of this type are particularly useful for structure determination using electron microscopy and computer image refinement. Three dimensional (3D) structural information can be derived from these crystals by computer reconstruction of photographs of toxin crystals taken at different tilt angles. Such 3D reconstructions may help elucidate the mechanism of entry of the enzymatic subunit of toxins into cells, particularly since these crystals form directly on a membrane interface at similar concentrations of ganglioside GT1 to the natural cellular receptors.

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