• Applied Microscopy
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• 제47권4호
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• pp.215-217
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• 2017

Dr. Jacques Dubochet, Dr. Joachim Frank, and Dr. Richard Henderson received the 2017 Nobel Prize for Chemistry for their efforts to develop effective ways to obtain high-resolution three-dimensional images of biomolecules using cryo-electron microscopy. Congratulations to the Nobel Prize in the field of electron microscopy, I will explain the scientific contributions of the three winners and introduce the role of cryo-electron microscopy (including cryo technology) in biology.

• Applied Microscopy
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• 제46권1호
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• pp.1-5
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• 2016

Recent cryo-electron microscopy (EM) studies reported the structure of various types of proteins at high resolution which is sufficient to visualize the intermolecular interaction at near atomic level. There are two main factors that cause the advances in cryo-EM; the development of image processing techniques, such as single particle analysis, and the improved electron detection devices. Although the atomic structures of small and asymmetric proteins are not yet to be determined by cryo-EM, this striking improvement implies the bright prospect of the application in biomedical studies. This study reviews the recently published studies reported high resolution structures using improved imaging analysis techniques and electron detectors. Furthermore, we will discuss about the future aspects of cryo-EM application.

• 한국공작기계학회:학술대회논문집
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• 한국공작기계학회 2005년도 춘계학술대회 논문집
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• pp.15-18
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• 2005

We have designed and fabricated a thermal scanning electron microscopy. It includes an electron source, two condenser lenses, one objective lens, a scanning coil and a stigmator coil for focusing in column and also have a secondary electron detector for constructing the image in chamber with a high vacuum condition and control part for operating the SEM. Especially, in order for us to find out the optical characteristics, our attention and studies have been concentrated on the effects of two condenser lenses and one objective lens for high resolution with SEM. Finally, we developed a high resolution thermal scanning electron microscopy.

• 한국세라믹학회지
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• 제26권2호
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• pp.276-288
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• 1989

Interpretation of high-resolution transmission electron microscopy images of defects and complex structures such as found in ceramics generally requires matching of the images with compound image simulations for reliable interpretation. A transmission electron microscopy study of the aluminum oxide was carried out at high-resolution, so that the crystal structure of the aluminum oxide could be modelled on an atomic level. In conjunction with computer simulation comparisons, the images reveal directly the atomic structure of the oxide. Results show that comparison between experimental high-resolution electron microscopy images and simulated images leads to a one to one correspondence of the image to the atomic model of the aluminum oxide. The aluminum atoms are disordered in the octahedral sites and the tetrahedral sites in the spinel aluminum oxide.

• Applied Microscopy
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• 제45권2호
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• pp.89-94
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• 2015

This article briefly reviews the results of recently reported research on high-temperature Pb-free solder alloys and the research trend for characterization of the interfacial reaction layer. To improve the product reliability of high-temperature Pb-free solder alloys, thorough research is necessary not only to enhance the alloy properties but also to characterize and understand the interfacial reaction occurring during and after the bonding process. Transmission electron microscopy analysis is expected to play an important role in the development of high-temperature solders by providing accurate and reliable data with a high spatial resolution and facilitating understanding of the interfacial reaction at the solder joint.

• Applied Microscopy
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• 제44권4호
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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.

• Applied Microscopy
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• 제47권4호
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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.

• Applied Microscopy
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• 제36권spc1호
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• pp.1-7
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• 2006

The three-dimensional structure of an inorganic crystal, $SmZn_{0.67}Sb_2$ (space group $P4/nmm,\;a=4.30(3){\AA}\;and\;c= 10.27(1){\AA}$), was refined by electron crystallography utilizing high voltage electron microscopy (HVEM). Effects of instrumental resolution, image quality, beam damage and specimen tilting on the structure refinement have been evaluated. The instrumental resolution and image quality were the most important factors on the final results in the structure refinement, while the beam damage and specimen tilting effects could be experimentally minimized or controlled. The average phase errors $({\Phi}_{res})$ for the [001], [100] and [110] HVEM images of $SmZn_{0.67}Sb_2$ were $10.1^{\circ},\;9.6^{\circ}\;and\;6.8^{\circ}$, respectively. The atomic coordinates of $SmZn_{0.67}Sb_2$ were consistent within $0.0013{\AA}{\sim}0.0088{\AA}$, compared to the X-ray crystallography data for the same sample.

• Applied Microscopy
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• 제47권4호
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• pp.226-232
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• 2017

Electron microscopy and X-ray diffraction have together played a key role in our understanding of the molecular structure and mechanism of contraction of muscle. This review highlights the role of electron microscopy, from early insights into thick and thin filament structure by negative staining, to studies of single myosin molecule structure, and finally to recent high-resolution structures by cryo-electron microscopy. Muscle filaments are designed for movement. Their labile structures thus present challenges to obtaining near-atomic detail, which are also discussed.

• Applied Microscopy
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• 제47권4호
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• pp.223-225
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• 2017

Cryo-electron microscopy (cryo-EM) is arguably the most powerful tool used in structural biology. It is an important analytical technique that is used for gaining insight into the functional and molecular mechanisms of biomolecules involved in several physiological processes. Cryo-EM can be separated into the following three groups according to the analytical purposes and the features of the biological samples: cryo-electron tomography (cryo-ET), cryo-single-particle reconstruction, and cryo-electron crystallography. Cryo-tomography is a unique EM technique that is used to study intact biomolecular complexes within their original environments; it can provide mechanistic insights that are challenging for other EM-methods. However, the resolution of reconstructed three-dimensional (3D) models generated by cryo-ET is relatively low, while single-particle reconstruction can reproduce biomolecular structures having near-atomic resolution without the need for crystallization unless the samples are large (>200 kDa) and highly symmetrical. Cryo-electron crystallography is subdivided into the following two categories according to the types of samples: one category that deals with two-dimensional (2D) crystalline arrays and the other category that uses 3D crystals. These two categories of electron-crystallographic techniques use different diffraction data obtained from still diffraction and continuous-rotation diffraction. In this paper, we review crystal-based cryo-EM techniques and focus on the recently developed 3D electron-crystallographic technique called microcrystal-electron diffraction.