Three-dimensional imaging of dislocations by X-ray diffraction laminography

2012 ◽  
Vol 101 (24) ◽  
pp. 244103 ◽  
Author(s):  
D. Hänschke ◽  
L. Helfen ◽  
V. Altapova ◽  
A. Danilewsky ◽  
T. Baumbach
Keyword(s):  
Three Dimensional ◽  
X Ray Diffraction ◽  
Three Dimensional Imaging ◽  
X Ray

scholarly journals Three-dimensional Imaging of Nanoscale Internal Structure by Coherent X-ray Diffraction Microscope

Materia Japan ◽  
2007 ◽  
Vol 46 (12) ◽  
pp. 827-827
Author(s):  
Yoshinori Nishino ◽  
Yukio Takahashi ◽  
Tetsuya Ishikawa ◽  
Eiichiro Matsubara
Keyword(s):  
Internal Structure ◽  
Three Dimensional ◽  
X Ray Diffraction ◽  
Three Dimensional Imaging ◽  
X Ray

Development of an apparatus for Bragg coherent X-ray diffraction imaging, and its application to the three dimensional imaging of BaTiO3 nano-crystals

2019 ◽  
Vol 58 (SL) ◽  
pp. SLLA05 ◽  
Author(s):  
Kenji Ohwada ◽  
Kento Sugawara ◽  
Tomohiro Abe ◽  
Tetsuro Ueno ◽  
Akihiko Machida ◽  
...  
Keyword(s):  
Three Dimensional ◽  
X Ray Diffraction ◽  
Three Dimensional Imaging ◽  
X Ray ◽  
Diffraction Imaging

scholarly journals Report on a project on three-dimensional imaging of the biological cell by single-particle X-ray diffraction

2007 ◽  
Vol 64 (1) ◽  
pp. 33-35 ◽  
Author(s):  
D. Sayre
Keyword(s):  
Single Particle ◽  
High Vacuum ◽  
Three Dimensional ◽  
X Rays ◽  
X Ray Diffraction ◽  
Acta Cryst ◽  
Three Dimensional Imaging ◽  
X Ray ◽  
X Ray Crystallography ◽  
A Cell

Single-particle X-ray diffraction is an extension of X-ray crystallography which allows the specimen to be any small solid-state bounded object; in Shapiroet al.[Proc. Natl Acad. Sci. USA(2005),102, 15343–15346] and Thibaultet al.[Acta Cryst.(2006), A62, 248–261], the reader can find descriptions of a recent StonyBrook/Berkeley/Cornell two-dimensional imaging of a yeast cell by this technique. Our present work is aimed at extending the technique to the three-dimensional imaging of a cell. However, the usual method of doing that, namely rotating the specimen into many orientations in the X-ray beam, has not as yet given sufficiently good three-dimensional diffraction data to allow the work to go forward, the largest problem being the difficulty of preventing unwanted levels of change in the specimen through the extended exposure to a hostile environment of X-rays and, in some cases, high vacuum and/or extreme cold. The present paper discusses possible methods of dealing with this problem.

scholarly journals Report on a project on three-dimensional imaging of the biological cell by single-particle X-ray diffraction. Addendum

2007 ◽  
Vol 64 (1) ◽  
pp. 36-37 ◽  
Author(s):  
David A. Shapiro
Keyword(s):  
Three Dimensional ◽  
Biological Cell ◽  
X Ray Diffraction ◽  
Short Term ◽  
Acta Cryst ◽  
Three Dimensional Imaging ◽  
X Ray ◽  
Structural Problems ◽  
Material Sciences ◽  
Diffraction Microscopy

In the paper by Sayre [Acta Cryst.(2008), A64, 33–35], a proposal is made to use stereoscopy as a short-term means of overcoming the primarily technological hurdles involved in three-dimensional imaging of the biological cell by soft X-ray diffraction microscopy. This addendum provides a broader perspective on the techniques used by this rapidly maturing community to investigate structural problems in the biological and material sciences.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

scholarly journals An investigation of polyhedral deformation in two mixed-metal diarsenates: SrZnAs2O7and BaCuAs2O7

2015 ◽  
Vol 71 (4) ◽  
pp. 330-337 ◽  
Author(s):  
Sabina Kovač ◽  
Ljiljana Karanović ◽  
Tamara Đorđević
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
General Formula ◽  
Three Dimensional ◽  
X Ray Diffraction ◽  
Hydrothermal Conditions ◽  
X Ray ◽  
Open Framework ◽  
Geometrical Characteristics ◽  
Barium Copper

Two isostructural diarsenates, SrZnAs2O7(strontium zinc diarsenate), (I), and BaCuAs2O7[barium copper(II) diarsenate], (II), have been synthesized under hydrothermal conditions and characterized by single-crystal X-ray diffraction. The three-dimensional open-framework crystal structure consists of corner-sharingM2O5(M2 = Zn or Cu) square pyramids and diarsenate (As2O7) groups. Each As2O7group shares its five corners with five differentM2O5square pyramids. The resulting framework delimits two types of tunnels aligned parallel to the [010] and [100] directions where the large divalent nine-coordinatedM1 (M1 = Sr or Ba) cations are located. The geometrical characteristics of theM1O9,M2O5and As2O7groups of known isostructural diarsenates, adopting the general formulaM1IIM2IIAs2O7(M1II= Sr, Ba, Pb;M2II= Mg, Co, Cu, Zn) and crystallizing in the space groupP21/n, are presented and discussed.

A new model for packing of type-I collagen molecules in the native fibril

1981 ◽  
Vol 1 (10) ◽  
pp. 801-810 ◽  
Author(s):  
Karl A. Piez ◽  
Benes L. Trus
Keyword(s):  
Type I Collagen ◽  
Hexagonal Lattice ◽  
Three Dimensional ◽  
Equatorial Region ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Left Handed ◽  
Crystal Model ◽  
Collagen Molecules

A specific fibril model is presented consisting of bundles of five-stranded microfibrils, which are usually disordered (except axially) but under lateral compression become ordered. The features are as follows (where D = 234 residues or 67 nm): (1) D-staggered collagen molecules 4.5 D long in the helical microfibril have a left-handed supercoil with a pitch of 400–700 residues, but microfibrils need not have helical symmetry. (2) Straight-tilted 0.5-D overlap regions on a near-hexagonal lattice contribute the discrete x-ray diffraction reflections arising from lateral order, while the gap regions remain disordered. (3) The overlap regions are equivalent, but are crystallographically distinguished by systematic displacements from the near-hexagonal lattice. (4) The unit cell is the same as in a recently proposed three-dimensional crystal model, and calculated intensities in the equatorial region of the x-ray diffraction pattern agree with observed values.

scholarly journals Acemetacin cocrystals and salts: structure solution from powder X-ray data and form selection of the piperazine salt

IUCrJ ◽  
2014 ◽  
Vol 1 (2) ◽  
pp. 136-150 ◽  
Author(s):  
Palash Sanphui ◽  
Geetha Bolla ◽  
Ashwini Nangia ◽  
Vladimir Chernyshev
Keyword(s):  
Hydrogen Bonds ◽  
Dissolution Rate ◽  
Aqueous Medium ◽  
Acid Amide ◽  
Three Dimensional ◽  
X Ray Diffraction ◽  
Reference Drug ◽  
X Ray ◽  
Time Period ◽  
Solid Form

Acemetacin (ACM) is a non-steroidal anti-inflammatory drug (NSAID), which causes reduced gastric damage compared with indomethacin. However, acemetacin has a tendency to form a less soluble hydrate in the aqueous medium. We noted difficulties in the preparation of cocrystals and salts of acemetacin by mechanochemical methods, because this drug tends to form a hydrate during any kind of solution-based processing. With the objective to discover a solid form of acemetacin that is stable in the aqueous medium, binary adducts were prepared by the melt method to avoid hydration. The coformers/salt formers reported are pyridine carboxamides [nicotinamide (NAM), isonicotinamide (INA), and picolinamide (PAM)], caprolactam (CPR),p-aminobenzoic acid (PABA), and piperazine (PPZ). The structures of an ACM–INA cocrystal and a binary adduct ACM–PABA were solved using single-crystal X-ray diffraction. Other ACM cocrystals, ACM–PAM and ACM–CPR, and the piperazine salt ACM–PPZ were solved from high-resolution powder X-ray diffraction data. The ACM–INA cocrystal is sustained by the acid...pyridine heterosynthon and N—H...O catemer hydrogen bonds involving the amide group. The acid...amide heterosynthon is present in the ACM–PAM cocrystal, while ACM–CPR contains carboxamide dimers of caprolactam along with acid–carbonyl (ACM) hydrogen bonds. The cocrystals ACM–INA, ACM–PAM and ACM–CPR are three-dimensional isostructural. The carboxyl...carboxyl synthon in ACM–PABA posed difficulty in assigning the position of the H atom, which may indicate proton disorder. In terms of stability, the salts were found to be relatively stable in pH 7 buffer medium over 24 h, but the cocrystals dissociated to give ACM hydrate during the same time period. The ACM–PPZ salt and ACM–nicotinamide cocrystal dissolve five times faster than the stable hydrate form, whereas the ACM–PABA adduct has 2.5 times faster dissolution rate. The pharmaceutically acceptable piperazine salt of acemetacin exhibits superior stability, faster dissolution rate and is able to overcome the hydration tendency of the reference drug.

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