Mechanism of RNA Double Helix-Propagation at Atomic Resolution†

2009 ◽  
Vol 113 (9) ◽  
pp. 2614-2623 ◽  
Author(s):  
Srividya Mohan ◽  
Chiaolong Hsiao ◽  
Halena VanDeusen ◽  
Ryan Gallagher ◽  
Eric Krohn ◽  
...  
Keyword(s):  
Double Helix ◽  
Atomic Resolution ◽  
Helix Propagation

scholarly journals The molecular structure of the left-handed Z-DNA double helix at 1.0-Å atomic resolution

1989 ◽  
Vol 264 (14) ◽  
pp. 7921-7935
Author(s):  
R V Gessner ◽  
C A Frederick ◽  
G J Quigley ◽  
A Rich ◽  
A H J Wang
Keyword(s):  
Molecular Structure ◽  
Double Helix ◽  
Atomic Resolution ◽  
Left Handed ◽  
Z Dna ◽  
Dna Double Helix

Double Helix at Atomic Resolution

Nature ◽  
1973 ◽  
Vol 243 (5403) ◽  
pp. 150-154 ◽  
Author(s):  
JOHN M. ROSENBERG ◽  
NADRIAN C. SEEMAN ◽  
JUNG JA PARK KIM ◽  
F. L. SUDDATH ◽  
HUGH B. NICHOLAS ◽  
...  
Keyword(s):  
Double Helix ◽  
Atomic Resolution

An Amylose Antiparallel Double Helix at Atomic Resolution

Science ◽  
1987 ◽  
Vol 238 (4824) ◽  
pp. 205-208 ◽  
Author(s):  
W. HINRICHS ◽  
G. BUTTNER ◽  
M. STEIFA ◽  
CH. BETZEL ◽  
V. ZABEL ◽  
...  
Keyword(s):  
Double Helix ◽  
Atomic Resolution

scholarly journals Preferred orientation in an angled intercalation site of a chloro-substituted Λ -[Ru(TAP) 2 (dppz)] 2+ complex bound to d(TCGGCGCCGA) 2

2013 ◽  
Vol 371 (1995) ◽  
pp. 20120525 ◽  
Author(s):  
James P. Hall ◽  
Hanna Beer ◽  
Katrin Buchner ◽  
David J. Cardin ◽  
Christine J. Cardin
Keyword(s):  
Crystal Structure ◽  
Ruthenium Complex ◽  
Double Helix ◽  
Minor Groove ◽  
Preferred Orientation ◽  
Atomic Resolution ◽  
Oligonucleotide Duplex ◽  
First Time

The crystal structure of the ruthenium DNA ‘light-switch’ complex Λ -[Ru(TAP) 2 (11-Cl-dppz)] 2+ (TAP=tetraazaphenanthrene, dppz=dipyrido[3,2- a ′:2′,3′- c ]phenazine) bound to the oligonucleotide duplex d(TCGGCGCCGA) 2 is reported. The synthesis of the racemic ruthenium complex is described for the first time, and the racemate was used in this study. The crystal structure, at atomic resolution (1.0 Å), shows one ligand as a wedge in the minor groove, resulting in the 51 ° kinking of the double helix, as with the parent Λ -[Ru(TAP) 2 (dppz)] 2+ . Each complex binds to one duplex by intercalation of the dppz ligand and also by semi-intercalation of one of the orthogonal TAP ligands into a second symmetrically equivalent duplex. The 11-chloro substituent binds with the major component (66%) oriented with the 11-chloro substituent on the purine side of the terminal step of the duplex.

Imaging Molecules and Cells with the Atomic Force Microscope

1990 ◽  
Vol 48 (1) ◽  
pp. 254-255
Author(s):  
C.B. Prater ◽  
A.L. Weisenhorn ◽  
B. Dixon Northern ◽  
C.M. Peterson ◽  
S.A.C. Gould ◽  
...  
Keyword(s):  
Atomic Force Microscope ◽  
Natural Zeolite ◽  
Blood Clotting ◽  
Double Helix ◽  
Atomic Resolution ◽  
Biological Processes ◽  
Major Groove ◽  
Double Stranded Dna ◽  
Atomic Force ◽  
Amino Acid Polymers

The atomic force microscope (AFM) gives topographic images by scanning a sharp stylus over a surface. The stylus is attached to a spring lever which is deflected when the stylus interacts with the surface. The AFM images a surface by measuring deflection as a function of position over the surface. The AFM has given atomic resolution images of both conductors and nonconductors. The AFM has also given images of amino acid polymers with subnanometer resolution. The AFM has imaged samples covered with a liquid and biological processes like blood clotting have been imaged. In this report we present several images that demonstrate the variety of samples that can be imaged with the AFM.The AFM has imaged adsorbed molecules at subnanometer resolution. Figure 1A is an image of the bare (010) surface of the natural zeolite, clinoptilolite. Molecules of t-butanol were then adsorbed onto the surface from the liquid and the sample was imaged again (Fig. IB).Figure 2 is an image of double stranded DNA dried onto mica. The resolution is sufficient to reveal corrugation due to the major groove of the double helix. We are currently working to gain resolution sufficient to sequence single-stranded DNA.

Double Helix at Atomic Resolution

2018 ◽  
pp. 88-92
Author(s):  
JOHN M. ROSENBERG ◽  
NADRIAN C. SEEMAN ◽  
JUNG JA PARK KIM ◽  
F. L. SUDDATH ◽  
HUGH B. NICHOLAS ◽  
...  
Keyword(s):  
Double Helix ◽  
Atomic Resolution

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

Effect of strain on ADF-STEM high-resolution images

1991 ◽  
Vol 49 ◽  
pp. 666-667
Author(s):  
M. Kelly ◽  
D.M. Bird
Keyword(s):  
High Resolution ◽  
Strong Influence ◽  
Intensity Variation ◽  
Dark Field ◽  
Atomic Resolution ◽  
Strain Fields ◽  
High Resolution Image ◽  
Annular Dark Field ◽  
High Resolution Images ◽  
Interesting Alternative

It is well known that strain fields can have a strong influence on the details of HREM images. This, for example, can cause problems in the analysis of edge-on interfaces between lattice mismatched materials. An interesting alternative to conventional HREM imaging has recently been advanced by Pennycook and co-workers where the intensity variation in the annular dark field (ADF) detector is monitored as a STEM probe is scanned across the specimen. It is believed that the observed atomic-resolution contrast is correlated with the intensity of the STEM probe at the atomic sites and the way in which this varies as the probe moves from cell to cell. As well as providing a directly interpretable high-resolution image, there are reasons for believing that ADF-STEM images may be less suseptible to strain than conventional HREM. This is because HREM images arise from the interference of several diffracted beams, each of which is governed by all the excited Bloch waves in the crystal.

Electron crystallographic determination of the 3-D structure of staurolite at atomic resolution

1991 ◽  
Vol 49 ◽  
pp. 540-541
Author(s):  
Kenneth H. Downing ◽  
Hu Meisheng ◽  
Hans-Rudolf Went ◽  
Michael A. O'Keefe
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
High Resolution Electron Microscopy ◽  
Atomic Resolution ◽  
Dimensional Structure ◽  
Structure Information ◽  
Resolution Electron ◽  
Scattering Effects ◽  
High Resolution Images ◽  
Effects Of Radiation

With current advances in electron microscope design, high resolution electron microscopy has become routine, and point resolutions of better than 2Å have been obtained in images of many inorganic crystals. Although this resolution is sufficient to resolve interatomic spacings, interpretation generally requires comparison of experimental images with calculations. Since the images are two-dimensional representations of projections of the full three-dimensional structure, information is invariably lost in the overlapping images of atoms at various heights. The technique of electron crystallography, in which information from several views of a crystal is combined, has been developed to obtain three-dimensional information on proteins. The resolution in images of proteins is severely limited by effects of radiation damage. In principle, atomic-resolution, 3D reconstructions should be obtainable from specimens that are resistant to damage. The most serious problem would appear to be in obtaining high-resolution images from areas that are thin enough that dynamical scattering effects can be ignored.

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