3D nanoscale imaging of biological samples with laboratory-based soft X-ray sources

2015 ◽  
Author(s):  
Aurélie Dehlinger ◽  
Anne Blechschmidt ◽  
Daniel Grötzsch ◽  
Robert Jung ◽  
Birgit Kanngießer ◽  
...  
Keyword(s):  
Biological Samples ◽  
X Ray ◽  
Nanoscale Imaging

Artefacts in the x-ray microanalysis of frozen-hydrated biological samples

1987 ◽  
Vol 45 ◽  
pp. 658-659
Author(s):  
Patrick Echlin
Keyword(s):  
Electron Scattering ◽  
Biological Samples ◽  
Fracture Face ◽  
Detailed Structure ◽  
X Ray ◽  
Morphological Appearance ◽  
The Poor ◽  
Freeze Dried

A number of papers have appeared recently which purport to have carried out x-ray microanalysis on fully frozen hydrated samples. It is important to establish reliable criteria to be certain that a sample is in a fully hydrated state. The morphological appearance of the sample is an obvious parameter because fully hydrated samples lack the detailed structure seen in their freeze dried counterparts. The electron scattering by ice within a frozen-hydrated section and from the surface of a frozen-hydrated fracture face obscures cellular detail. (Fig. 1G and 1H.) However, the morphological appearance alone can be quite deceptive for as Figures 1E and 1F show, parts of frozen-dried samples may also have the poor morphology normally associated with fully hydrated samples. It is only when one examines the x-ray spectra that an assurance can be given that the sample is fully hydrated.

scholarly journals Principles of Different X-ray Phase-Contrast Imaging: A Review

2021 ◽  
Vol 11 (7) ◽  
pp. 2971
Author(s):  
Siwei Tao ◽  
Congxiao He ◽  
Xiang Hao ◽  
Cuifang Kuang ◽  
Xu Liu
Keyword(s):  
Biological Samples ◽  
Phase Contrast ◽  
Recent Progress ◽  
Phase Contrast Imaging ◽  
Contrast Imaging ◽  
X Ray ◽  
X Ray Imaging ◽  
Internal Structures ◽  
X Ray Absorption ◽  
Made In

Numerous advances have been made in X-ray technology in recent years. X-ray imaging plays an important role in the nondestructive exploration of the internal structures of objects. However, the contrast of X-ray absorption images remains low, especially for materials with low atomic numbers, such as biological samples. X-ray phase-contrast images have an intrinsically higher contrast than absorption images. In this review, the principles, milestones, and recent progress of X-ray phase-contrast imaging methods are demonstrated. In addition, prospective applications are presented.

scholarly journals A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter

2012 ◽  
Vol 46 (1) ◽  
pp. 234-241 ◽  
Author(s):  
Chae Un Kim ◽  
Jennifer L. Wierman ◽  
Richard Gillilan ◽  
Enju Lima ◽  
Sol M. Gruner
Keyword(s):  
High Pressure ◽  
Biological Samples ◽  
Protein Crystal ◽  
High Background ◽  
X Ray ◽  
Coherent Diffraction Imaging ◽  
X Ray Scattering ◽  
Alternative Method ◽  
Helium Gas ◽  
Diffraction Imaging

High-pressure cryocooling has been developed as an alternative method for cryopreservation of macromolecular crystals and successfully applied for various technical and scientific studies. The method requires the preservation of crystal hydration as the crystal is pressurized with dry helium gas. Previously, crystal hydration was maintained either by coating crystals with a mineral oil or by enclosing crystals in a capillary which was filled with crystallization mother liquor. These methods are not well suited to weakly diffracting crystals because of the relatively high background scattering from the hydrating materials. Here, an alternative method of crystal hydration, called capillary shielding, is described. The specimen is kept hydratedviavapor diffusion in a shielding capillary while it is being pressure cryocooled. After cryocooling, the shielding capillary is removed to reduce background X-ray scattering. It is shown that, compared to previous crystal-hydration methods, the new hydration method produces superior crystal diffraction with little sign of crystal damage. Using the new method, a weakly diffracting protein crystal may be properly pressure cryocooled with little or no addition of external cryoprotectants, and significantly reduced background scattering can be observed from the resulting sample. Beyond the applications for macromolecular crystallography, it is shown that the method has great potential for the preparation of noncrystalline hydrated biological samples for coherent diffraction imaging with future X-ray sources.

scholarly journals 1P291 Humidity-controlled preparation of frozen-hydrated biological samples for cryogenic coherent X-ray diffraction imaging using XFEL(27. Bioimaging,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S154
Author(s):  
Yuki Takayama ◽  
Masayoshi Nakasako ◽  
Tomotaka Oroguchi ◽  
Yuki Sekiguchi ◽  
Amane Kobayashi ◽  
...  
Keyword(s):  
Biological Samples ◽  
X Ray Diffraction ◽  
X Ray ◽  
Diffraction Imaging ◽  
Controlled Preparation

scholarly journals Application of the Gatan X-ray Ultramicroscope (XuM) to the Investigation of Material and Biological Samples

2008 ◽  
Vol 16 (6) ◽  
pp. 14-17 ◽  
Author(s):  
Paul Mainwaring
Keyword(s):  
Sample Size ◽  
Spatial Resolution ◽  
Biological Samples ◽  
Easy Access ◽  
X Ray ◽  
Analytical Functions ◽  
Important Development ◽  
X Ray Imaging ◽  
Sem Imaging ◽  
Power Capability

X-ray ultramicroscopy in the SEM is a relatively new application in the wider field of X-ray microscopy. This latter field includes synchrotron and cabinet-based systems that vary in their X-ray power, capability, sample size, spatial resolution, and convenience. One important capability of the SEM-hosted X-ray microscope is that the normal SEM imaging and analytical functions such as secondary and backscattered imaging and microanalysis by EDX or WDS are unimpeded. X-ray imaging then serves as a complement to the normal use of the SEM. The convenience of easy access in an SEM lab to an X-ray microscope with 3D tomographic capability makes this an important development.

Nanoscale Imaging Using Coherent and Incoherent Laboratory Based Soft X-Ray Sources

2015 ◽  
pp. 267-273
Author(s):  
H. Stiel ◽  
A. Dehlinger ◽  
K.A. Janulewicz ◽  
R. Jung ◽  
H. Legall ◽  
...  
Keyword(s):  
X Ray ◽  
Nanoscale Imaging

scholarly journals Time-Resolved X-Ray Microscopy for Materials Science

2019 ◽  
Vol 49 (1) ◽  
pp. 389-415 ◽  
Author(s):  
Haidan Wen ◽  
Mathew J. Cherukara ◽  
Martin V. Holt
Keyword(s):  
Large Scale ◽  
Materials Science ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Imaging ◽  
Materials Research ◽  
Microscopic Studies ◽  
Nanoscale Imaging ◽  
Indispensable Tool ◽  
The Time Domain

X-ray microscopy has been an indispensable tool to image nanoscale properties for materials research. One of its recent advances is extending microscopic studies to the time domain to visualize the dynamics of nanoscale phenomena. Large-scale X-ray facilities have been the powerhouse of time-resolved X-ray microscopy. Their upgrades, including a significant reduction of the X-ray emittance at storage rings (SRs) and fully coherent ultrashort X-ray pulses at free-electron lasers (FELs), will lead to new developments in instrumentation and will open new scientific opportunities for X-ray imaging of nanoscale dynamics with the simultaneous attainment of unprecedentedly high spatial and temporal resolutions. This review presents recent progress in and the outlook for time-resolved X-ray microscopy in the context of ultrafast nanoscale imaging and its applications to condensed matter physics and materials science.

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