scholarly journals Automated Projection Spectroscopy (APSY) for the Assignment of NMR Resonances of Biological Macromolecules

2012 ◽  
Vol 66 (10) ◽  
pp. 770-774 ◽  
Author(s):  
Barbara Krähenbühl ◽  
Gerhard Wider
Keyword(s):  
Biological Macromolecules ◽  
Projection Spectroscopy ◽  
Automated Projection Spectroscopy

Automated projection spectroscopy in solid-state NMR

2018 ◽  
Vol 72 (3-4) ◽  
pp. 163-170 ◽  
Author(s):  
Alexander Klein ◽  
Suresh K. Vasa ◽  
Rasmus Linser
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Projection Spectroscopy ◽  
Automated Projection Spectroscopy

scholarly journals Automated projection spectroscopy (APSY)

2005 ◽  
Vol 102 (31) ◽  
pp. 10876-10881 ◽  
Author(s):  
S. Hiller ◽  
F. Fiorito ◽  
K. Wuthrich ◽  
G. Wider
Keyword(s):  
Projection Spectroscopy ◽  
Automated Projection Spectroscopy

Observation of biological macromolecules using various electron microscopic methods

1978 ◽  
Vol 36 (2) ◽  
pp. 170-171
Author(s):  
Mitsuo Ohtsuki ◽  
Michael Sogard
Keyword(s):  
Electron Microscope ◽  
Phase Contrast ◽  
Image Interpretation ◽  
Density Lipoprotein ◽  
Biological Macromolecules ◽  
Contrast Effects ◽  
Biological Structure ◽  
Electron Microscopic ◽  
Structural Investigations ◽  
Staining Techniques

Structural investigations of biological macromolecules commonly employ CTEM with negative staining techniques. Difficulties in valid image interpretation arise, however, due to problems such as variability in thickness and degree of penetration of the staining agent, noise from the supporting film, and artifacts from defocus phase contrast effects. In order to determine the effects of these variables on biological structure, as seen by the electron microscope, negative stained macromolecules of high density lipoprotein-3 (HDL3) from human serum were analyzed with both CTEM and STEM, and results were then compared with CTEM micrographs of freeze-etched HDL3. In addition, we altered the structure of this molecule by digesting away its phospholipid component with phospholipase A2 and look for consistent changes in structure.

Measurement and Reduction of Radiation Damage in Frozen Hydrated Crystalline Specimens

1978 ◽  
Vol 36 (3) ◽  
pp. 70-77 ◽  
Author(s):  
R.M. Glaeser ◽  
S.B. Hayward
Keyword(s):  
Diffraction Pattern ◽  
Structural Information ◽  
Structural Disorder ◽  
Structural Features ◽  
Biological Macromolecules ◽  
Diffraction Intensity ◽  
Object Structure ◽  
Specimen Material ◽  
Unit Cells ◽  
Identical Unit

Highly ordered or crystalline biological macromolecules become severely damaged and structurally disordered after a brief electron exposure. Evidence that damage and structural disorder are occurring is clearly given by the fading and eventual disappearance of the specimen's electron diffraction pattern. The fading and disappearance of sharp diffraction spots implies a corresponding disappearance of periodic structural features in the specimen. By the same token, there is a oneto- one correspondence between the disappearance of the crystalline diffraction pattern and the disappearance of reproducible structural information that can be observed in the images of identical unit cells of the object structure. The electron exposures that result in a significant decrease in the diffraction intensity will depend somewhat upon the resolution (Bragg spacing) involved, and can vary considerably with the chemical makeup and composition of the specimen material.

Concentration determination of chromatin in unstained resin-embedded sections by means of Z-contrast in STEM

1990 ◽  
Vol 48 (2) ◽  
pp. 186-187
Author(s):  
M. Haider ◽  
B. Bohrmann
Keyword(s):  
Energy Loss ◽  
Freeze Substitution ◽  
Biological Macromolecules ◽  
Local Concentration ◽  
E Coli ◽  
Concentration Determination ◽  
Phosphorous Content ◽  
Z Contrast ◽  
Electron Energy Loss

The technique of Z-contrast in STEM offers the possibility to determine the local concentration of macromolecules like lipids, proteins or DNA. Contrast formation depends on the atomic composition of the particular structure. In the case of DNA, its phosphorous content discriminates it from other biological macromolecules. In our studies, sections of E. coli, the dinoflagellate Amphidinium carterae and Euglena spec. cells were used which were obtained by cryofixation followed by freeze-substitution into acetone with 3% glutaraldehyde. The samples were then embedded either in Lowicryl HM20 at low temperature or in Epon at high temperature. Sections were coated on both sides with 30Å carbon.The DF- and the inelastic image have been recorded simultaneously with a Cryo-STEM. This Cryo-STEM is equipped with a highly dispersive Electron Energy Loss Spectrometer. With this instrument pure Z-contrast can be achieved either with a Filtered DF-image divided by the inelastic image or, as is used in this paper, by dividing the conventional DF-image by an inelastic image which has been recorded with an inelastic detector whose response is dependent on the total energy loss of the inelastically scattered electrons.

Resolution assessment from spectral signal-to-noise ratios

1987 ◽  
Vol 45 ◽  
pp. 746-747
Author(s):  
M. Unser ◽  
B.L. Trus ◽  
A.C. Steven
Keyword(s):  
Electron Microscopy ◽  
Limiting Factor ◽  
Biological Macromolecules ◽  
Signal To Noise ◽  
Differential Phase ◽  
Traditional Measure ◽  
Spectral Signal ◽  
Two Measures ◽  
Diffraction Patterns ◽  
Averaging Techniques

Since the resolution-limiting factor in electron microscopy of biological macromolecules is not instrumental, but is rather the preservation of structure, operational definitions of resolution have to be based on the mutual consistency of a set of like images. The traditional measure of resolution for crystalline specimens in terms of the extent of periodic reflections in their diffraction patterns is such a criterion. With the advent of correlation averaging techniques for lattice rectification and the analysis of non-crystalline specimens, a more general - and desirably, closely compatible - resolution criterion is needed. Two measures of resolution for correlation-averaged images have been described, namely the differential phase residual (DPR) and the Fourier ring correlation (FRC). However, the values that they give for resolution often differ substantially. Furthermore, neither method relates in a straightforward way to the long-standing resolution criterion for crystalline specimens.

A TEM study of electron tunneling in biological macromolecules

1987 ◽  
Vol 45 ◽  
pp. 140-141
Author(s):  
J. A. Panitz
Keyword(s):  
Stark Effect ◽  
Electron Tunneling ◽  
Imaging Modality ◽  
Tunneling Current ◽  
Biological Species ◽  
Scanning Tunneling ◽  
Biological Macromolecules ◽  
Flat Surfaces ◽  
Virus Particles ◽  
Stm Images

Tunneling is a ubiquitous phenomenon. Alpha particle disintegration, the Stark effect, superconductivity in thin films, field-emission, and field-ionization are examples of electron tunneling phenomena. In the scanning tunneling microscope (STM) electron tunneling is used as an imaging modality. STM images of flat surfaces show structure at the atomic level. However, STM images of large biological species deposited onto flat surfaces are disappointing. For example, unstained virus particles imaged in the STM do not resemble their TEM counterparts.It is not clear how an STM image of a biological species is formed. Most biological species are large compared to the nominal electrode separation of ∼ 1nm that is required for electron tunneling. To form an image of a biological species, the tunneling electrodes must be separated by a distance that would normally be too large for a tunneling current to be observed.

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