• Title/Summary/Keyword: Electron crystallography

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Crystallography Analysis of the β-Mg17Al12 Precipitates by the Secondary Constrained Coincident Site Lattice Model

  • Huang, Xuefei;Huang, Weigang
    • Applied Microscopy
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    • v.45 no.4
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    • pp.230-235
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    • 2015
  • Crystallographic models are effective tools to interpret, calculate and even to predict the preferred crystallographic morphologies of precipitates in various precipitation systems. The present study gives an introduction on the recently developed secondary constrained coincident site lattice (II-CCSL) model. Using the II-CCSL model, the interface matching condition of the ${\beta}-Mg_{17}Al_{12}$ precipitates with ${\alpha}-Mg$ matrix in an aged AZ91 alloy has been analyzed to rationalize the morphologies of the precipitates. The results show that the characteristic crystallographic features of the observed ${\beta}-Mg_{17}Al_{12}$ precipitates, i.e., the habit plane of the ${\beta}-Mg_{17}Al_{12}$ lath with a Burgers orientation relationship (OR) and the growth direction of the ${\beta}-Mg_{17}Al_{12}$ with a Crawley OR exhibit a better lattice matching degree than their vicinal orientations. Moreover, the Crawley OR is preferred to the Burgers OR due to a better lattice match.

Structure-based Functional Discovery of Proteins: Structural Proteomics

  • Jung, Jin-Won;Lee, Weon-Tae
    • BMB Reports
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    • v.37 no.1
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    • pp.28-34
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    • 2004
  • The discovery of biochemical and cellular functions of unannotated gene products begins with a database search of proteins with structure/sequence homologues based on known genes. Very recently, a number of frontier groups in structural biology proposed a new paradigm to predict biological functions of an unknown protein on the basis of its three-dimensional structure on a genomic scale. Structural proteomics (genomics), a research area for structure-based functional discovery, aims to complete the protein-folding universe of all gene products in a cell. It would lead us to a complete understanding of a living organism from protein structure. Two major complementary experimental techniques, X-ray crystallography and NMR spectroscopy, combined with recently developed high throughput methods have played a central role in structural proteomics research; however, an integration of these methodologies together with comparative modeling and electron microscopy would speed up the goal for completing a full dictionary of protein folding space in the near future.

Three-dimensional Structure of Protein Using Electron Microscopy (전자현미경을 이용한 단백질 3차원 구조)

  • Cheong, Gang-Won
    • Applied Microscopy
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    • v.30 no.3
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    • pp.241-248
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    • 2000
  • Electron microscopy has used for analysing the structure of protein over 30 years. Bacteriohodopsin and porins are used as examples to illustrate the progress that has recently been made in attaining resolutions which hitherto were regarded as exclusive to the realm of x-ray crystallography. To determine a protein structure used by electron microscopy, one must pass through a number of basic steps including preparation of specimen , data acquisition and data processing.

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Transmission Electron Microscope Sampling Method for Three-Dimensional Structure Analysis of Two-Dimensional Soft Materials

  • Lee, Sang-Gil;Lee, Ji-Hyun;Yoo, Seung Jo;Datta, Suvo Jit;Hwang, In-Chul;Yoon, Kyung-Byung;Kim, Jin-Gyu
    • Applied Microscopy
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    • v.45 no.4
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    • pp.203-207
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    • 2015
  • Sample preparation is very important for crystal structure analysis of novel nanostructured materials in electron microscopy. Generally, a grid dispersion method has been used as transmission electron microscope (TEM) sampling method of nano-powder samples. However, it is difficult to obtain the cross-sectional information for the tabular-structured materials. In order to solve this problem, we have attempted a new sample preparation method using focused ion beam. Base on this approach, it was possible to successfully obtain the electron diffraction patterns and high-resolution TEM images of the cross-section of tabular structure. Finally, we were able to obtain three-dimensional crystallographic information of novel zeolite nano-crystal of the tabular morphology by applying the new sample preparation technique.

Circular Fast Fourier Transform Application: A Useful Script for Fast Fourier Transform Data Analysis of High-resolution Transmission Electron Microscopy Image

  • Kim, Jin-Gyu;Yoo, Seung Jo;Kim, Chang-Yeon;Jou, Hyeong-Tae
    • Applied Microscopy
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    • v.44 no.4
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    • pp.138-143
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    • 2014
  • Transmission electron microscope (TEM) is an excellent tool for studying the structure and properties of nanostructured materials. As the development of $C_s$-corrected TEM, the direct analysis of atomic structures of nanostructured materials can be performed in the high-resolution transmission electron microscopy (HRTEM). Especially, fast Fourier transform (FFT) technique in image processing is very useful way to determine the crystal structure of HRTEM images in reciprocal space. To apply FFT technique in HRTEM analysis in more reasonable and friendly manner, we made a new circular region of interest (C-ROI) FFT script and tested it for several HRTEM analysis. Consequentially, it was proved that the new FFT application shows more quantitative and clearer results than conventional FFT script by removing the streaky artifacts in FFT pattern images. Finally, it is expected that the new FFT script gives great advantages for quantitative interpretation of HRTEM images of many nanostructured materials.

Image Processing and Cryo-Transmission Electron Microscopy; Example of Human Proteasome

  • Choi, Hyosun;Jeon, Hyunbum;Noh, Seulgi;Kwon, Ohkyung;Mun, Ji Young
    • Applied Microscopy
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    • v.48 no.1
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    • pp.1-5
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    • 2018
  • Cryo-transmission electron microscopy (cryo-TEM) allows us to perform structural analysis of a analyses of large protein complexes, which are difficult to analyze using X-ray crystallography or nuclear magnetic resonance. The most common examples of proteins used are ribosomes and proteasomes. In this paper, we briefly describe the advantage of cryo-TEM and the process of two-dimensional classification by considering a human proteasome as an example.

The Nobel Prize in Chemistry 2017: High-Resolution Cryo-Electron Microscopy

  • Chung, Jae-Hee;Kim, Ho Min
    • Applied Microscopy
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    • v.47 no.4
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    • pp.218-222
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    • 2017
  • The 2017 Nobel Prize in Chemistry was awarded to the following three pioneers: Dr. Joachim Frank, Dr. Jacques Dubochet, and Dr. Richard Henderson. They all contributed to the development of a Cryo-electron microscopy (EM) technique for determining the high-resolution structures of biomolecules in solution, particularly without crystal and with much less amount of biomolecules than X-ray crystallography. In this brief commentary, we address the major advances made by these three Nobel laureates as well as the current status and future prospects of this Cryo-EM technique.

Purification and Single Crystal Growth of Molybdenum by Electron Beam Floating Zone Melting (Electron Beam Floating Zone Melting에 의한 몰리브덴의 정련 및 단결정 성장에 관한 연구)

  • 최용삼;지응준
    • Korean Journal of Crystallography
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    • v.3 no.2
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    • pp.85-97
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    • 1992
  • EBFZM( Electron Beam Floating Zone Melting) 법을 이용하여 몰리브덴에서의 금속계 불순물과 침입형 불순물의 정련기구 및 단결정 성장기구를 연구하 였다. Fe, Cr, Co등의 금속계 불순물은 몰리브덴과의 평형증기압의 차이에 따른 불순물의 선택적 증발에 의하여 우수한 정련효과를 나타내며, 몰리브덴보다 응점이 높은 Ta, W는 잘 제거되지 않았다. 한편 대역 정제에 의한 정련효과는 미약함을 확인하였다. EBF ZM은 C,0,N등의 침입형 불순물의 정련에도 효과적 이었다. 본 연구의 모든 조건에서 몰리브덴은 단결정으로 성장하였으며 2차 재결정 epitaxy에 의한 단결 정 성장기구가 제시되었다. 몰리브덴 단결정 내의 전 위밀도는 strain-anneal법에 의한 단결정의 경우보다 높았으며,본 실험의 열처리 조건에서는 변화하지 않았다. The purification and single crystal growth mechanisms of molybdenum were analysed in EBFZM ( electron beam floating zone melting). Metallic impurities of Fe, Cr, Co were purified efficiently but Ta and W were not removed well in this study. It was due to a preferential evaporation of the elements caused by the difference in equillibrium vapor pressure between the elements and molybdenum. The pu- rification effect by zone refining was not significant. The EBFZM also refined the interstitial impurities of C, 0 and N, effectively. The single crystals of molybdenum were grown regardless of the experimental conditions and the secondary recrystallization epitaxy was surge sled as a growth mechanism. The dislocation density in single crystal was higher than that by strain-anneal method, and was not reduced by heat treatments.

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Atomic structure and crystallography of joints in SnO2 nanowire networks

  • Hrkac, Viktor;Wolff, Niklas;Duppel, Viola;Paulowicz, Ingo;Adelung, Rainer;Mishra, Yogendra Kumar;Kienle, Lorenz
    • Applied Microscopy
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    • v.49
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    • pp.1.1-1.10
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    • 2019
  • Joints of three-dimensional (3D) rutile-type (r) tin dioxide ($SnO_2$) nanowire networks, produced by the flame transport synthesis (FTS), are formed by coherent twin boundaries at $(101)^r$ serving for the interpenetration of the nanowires. Transmission electron microscopy (TEM) methods, i.e. high resolution and (precession) electron diffraction (PED), were utilized to collect information of the atomic interface structure along the edge-on zone axes $[010]^r$, $[111]^r$ and superposition directions $[001]^r$, $[101]^r$. A model of the twin boundary is generated by a supercell approach, serving as base for simulations of all given real and reciprocal space data as for the elaboration of three-dimensional, i.e. relrod and higher order Laue zones (HOLZ), contributions to the intensity distribution of PED patterns. Confirmed by the comparison of simulated and experimental findings, details of the structural distortion at the twin boundary can be demonstrated.

Synthesis and Characterization of 1-D BiSI and 2-D BiOI Nanostructures

  • Lee, Juheon;Min, Bong-Ki;Cho, Insu;Sohn, Youngku
    • Bulletin of the Korean Chemical Society
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    • v.34 no.3
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    • pp.773-776
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    • 2013
  • We have prepared 1-D BiSI and 2-D BiOI nanostructures, and characterized them by scanning electron microscopy, transmission electron microscopy (TEM), X-ray diffraction crystallography, thermogravimetric analysis/differential scanning calorimetry, and UV-visible absorption. Here, we first report clear HR-TEM image of BiSI. In addition, we first found that the growth direction of BiSI is [12-1] plane, with the neighboring distance of 0.30 nm. The crystal structures of BiSI and BiOI are found to be orthorhombic (Pnam) and tetragonal (P4/nmm), respectively. The absorption band gaps of BiSI and BiOI are measured to be 1.55 and 1.92 eV, respectively. Our study could further highlight the applications of V-VI-VII compounds.