Development of Quantitative X-Ray Microtomography

1990 ◽  
Vol 217 ◽  
Author(s):  
H. W. Deckman ◽  
J. H. Dunsmuir ◽  
K. L. D'Amico ◽  
S. R. Ferguson ◽  
B. P. Flannery
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
Imaging Modalities ◽  
Two Dimensional ◽  
Evolutionary Path ◽  
X Ray ◽  
Temporal And Spatial

ABSTRACTWe have developed several x-ray microtomography systems which function as quantitative three dimensional x-ray microscopes. In this paper we describe the evolutionary path followed from making the first high resolution experimental microscopes to later generations which can be routinely used for investigating materials. Developing the instrumentation for reliable quantitative x-ray microscopy using synchrotron and laboratory based x-ray sources has led to other imaging modalities for obtaining temporal and spatial two dimensional information.

High Resolution Synchrotron X-Ray Diffraction Tomography Of Large-Grained Samples

1996 ◽  
Vol 437 ◽  
Author(s):  
D.P. Piotrowski ◽  
S.R. Stock ◽  
A. Guvenilir ◽  
J.D. Haase ◽  
Z.U. Rek
Keyword(s):  
Spatial Distribution ◽  
High Resolution ◽  
Three Dimensional ◽  
Polycrystalline Materials ◽  
Diffraction Tomography ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
Image Storage ◽  
X Ray ◽  
Dimensional Distribution

AbstractIn order to understand the macroscopic response of polycrystalline structural materials to loading, it is frequently essential to know the spatial distribution of strain as well as the variation of micro-texture on the scale of 100 μm. The methods must be nondestructive, however, if the three-dimensional evolution of strain is to be studied. This paper describes an approach to high resolution synchrotron x-ray diffraction tomography of polycrystalline materials. Results from model samples of randomly-packed, millimeter-sized pieces of Si wafers and of similarly sized single-crystal Al blocks have been obtained which indicate that polychromatic beams collimated to 30 μm diameter can be used to determine the depth of diffracting volume elements within ± 70 μm. The variation in the two-dimensional distribution of diffracted intensity with changing sample to detector separation is recorded on image storage plates and used to infer the depth of diffracting volume elements.

High Resolution Microscopy of Multi-Layered Biological Crystals

1982 ◽  
Vol 40 ◽  
pp. 80-83
Author(s):  
H.A. Cohen ◽  
T.W. Jeng ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Low Dose ◽  
Three Dimensional ◽  
Data Interpretation ◽  
Two Dimensional ◽  
Biological Objects ◽  
Density Maps ◽  
Density Map ◽  
Complex Crystal ◽  
High Resolution Microscopy

This tutorial will discuss the methodology of low dose electron diffraction and imaging of crystalline biological objects, the problems of data interpretation for two-dimensional projected density maps of glucose embedded protein crystals, the factors to be considered in combining tilt data from three-dimensional crystals, and finally, the prospects of achieving a high resolution three-dimensional density map of a biological crystal. This methodology will be illustrated using two proteins under investigation in our laboratory, the T4 DNA helix destabilizing protein gp32*I and the crotoxin complex crystal.

Tubulin structure at intermediate resolution

1995 ◽  
Vol 53 ◽  
pp. 852-853
Author(s):  
K. H. Downing ◽  
S. G. Wolf ◽  
E. Nogales
Keyword(s):  
High Resolution ◽  
Structural Data ◽  
Therapeutic Drug ◽  
Zinc Ions ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray ◽  
Negative Stain ◽  
Functional Mechanisms ◽  
Tubulin Structure

Microtubules are involved in a host of critical cell activities, many of which involve transport of organelles through the cell. Different sets of microtubules appear to form during the cell cycle for different functions. Knowledge of the structure of tubulin will be necessary in order to understand the various functional mechanisms of microtubule assemble, disassembly, and interaction with other molecules, but tubulin has so far resisted crystallization for x-ray diffraction studies. Fortuitously, in the presence of zinc ions, tubulin also forms two-dimensional, crystalline sheets that are ideally suited for study by electron microscopy. We have refined procedures for forming the sheets and preparing them for EM, and have been able to obtain high-resolution structural data that sheds light on the formation and stabilization of microtubules, and even the interaction with a therapeutic drug.Tubulin sheets had been extensively studied in negative stain, demonstrating that the same protofilament structure was formed in the sheets and microtubules. For high resolution studies, we have found that the sheets embedded in either glucose or tannin diffract to around 3 Å.

Three-dimensional crystallization of membrane proteins

1988 ◽  
Vol 21 (4) ◽  
pp. 429-477 ◽  
Author(s):  
W. Kühlbrandt
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Biological Macromolecules ◽  
X Ray ◽  
X Ray Crystallography ◽  
Membrane Protein Complexes ◽  
Essential Prerequisite

As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

Three-dimensional analysis of plant structure using high-resolution X-ray computed tomography

2003 ◽  
Vol 8 (1) ◽  
pp. 2-6 ◽  
Author(s):  
Wolfgang H Stuppy ◽  
Jessica A Maisano ◽  
Matthew W Colbert ◽  
Paula J Rudall ◽  
Timothy B Rowe
Keyword(s):  
Computed Tomography ◽  
High Resolution ◽  
Dimensional Analysis ◽  
Three Dimensional ◽  
Plant Structure ◽  
X Ray ◽  
X Ray Computed

Three dimensional characterization of laser ablation craters using high resolution X-ray computed tomography

2018 ◽  
Vol 139 ◽  
pp. 75-82 ◽  
Author(s):  
A.H. Galmed ◽  
A. du Plessis ◽  
S.G. le Roux ◽  
E. Hartnick ◽  
H. Von Bergmann ◽  
...  
Keyword(s):  
Computed Tomography ◽  
Laser Ablation ◽  
High Resolution ◽  
Three Dimensional ◽  
X Ray ◽  
X Ray Computed

scholarly journals Low-Zpolymer sample supports for fixed-target serial femtosecond X-ray crystallography

2015 ◽  
Vol 48 (4) ◽  
pp. 1072-1079 ◽  
Author(s):  
Geoffrey K. Feld ◽  
Michael Heymann ◽  
W. Henry Benner ◽  
Tommaso Pardini ◽  
Ching-Ju Tsai ◽  
...  
Keyword(s):  
Protective Antigen ◽  
Three Dimensional ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
Fixed Target ◽  
X Ray ◽  
X Ray Crystallography ◽  
Transmission Electron ◽  
Linac Coherent Light Source ◽  
Efficient Alternative

X-ray free-electron lasers (XFELs) offer a new avenue to the structural probing of complex materials, including biomolecules. Delivery of precious sample to the XFEL beam is a key consideration, as the sample of interest must be serially replaced after each destructive pulse. The fixed-target approach to sample delivery involves depositing samples on a thin-film support and subsequent serial introductionviaa translating stage. Some classes of biological materials, including two-dimensional protein crystals, must be introduced on fixed-target supports, as they require a flat surface to prevent sample wrinkling. A series of wafer and transmission electron microscopy (TEM)-style grid supports constructed of low-Zplastic have been custom-designed and produced. Aluminium TEM grid holders were engineered, capable of delivering up to 20 different conventional or plastic TEM grids using fixed-target stages available at the Linac Coherent Light Source (LCLS). As proof-of-principle, X-ray diffraction has been demonstrated from two-dimensional crystals of bacteriorhodopsin and three-dimensional crystals of anthrax toxin protective antigen mounted on these supports at the LCLS. The benefits and limitations of these low-Zfixed-target supports are discussed; it is the authors' belief that they represent a viable and efficient alternative to previously reported fixed-target supports for conducting diffraction studies with XFELs.

Three Dimensional X-Ray Computed Tomography in Materials Science

MRS Bulletin ◽  
1988 ◽  
Vol 13 (1) ◽  
pp. 13-18 ◽  
Author(s):  
J.H. Kinney ◽  
Q.C. Johnson ◽  
U. Bonse ◽  
M.C. Nichols ◽  
R.A. Saroyan ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Sample Preparation ◽  
Visible Light ◽  
Three Dimensional ◽  
Materials Characterization ◽  
Imaging Technology ◽  
X Ray ◽  
X Ray Imaging ◽  
Visible Light Imaging

Imaging is the cornerstone of materials characterization. Until the middle of the present century, visible light imaging provided much of the information about materials. Though visible light imaging still plays an extremely important role in characterization, relatively low spatial resolution and lack of chemical sensitivity and specificity limit its usefulness.The discovery of x-rays and electrons led to a major advance in imaging technology. X-ray diffraction and electron microscopy allowed us to characterize the atomic structure of materials. Many materials vital to our high technology economy and defense owe their existence to the understanding of materials structure brought about with these high-resolution methods.Electron microscopy is an essential tool for materials characterization. Unfortunately, electron imaging is always destructive due to the sample preparation that must be done prior to imaging. Furthermore, electron microscopy only provides information about the surface of a sample. Three dimensional information, of great interest in characterizing many new materials, can be obtained only by time consuming sectioning of an object.The development of intense synchrotron light sources in addition to the improvements in solid state imaging technology is revolutionizing materials characterization. High resolution x-ray imaging is a potentially valuable tool for materials characterization. The large depth of x-ray penetration, as well as the sensitivity of absorption crosssections to atomic chemistry, allows x-ray imaging to characterize the chemistry of internal structures in macroscopic objects with little sample preparation. X-ray imaging complements other imaging modalities, such as electron microscopy, in that it can be performed nondestructively on metals and insulators alike.

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