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용액상의 단백질 구조 분석을 위한 PLS 4C1빔라인의 성능 테스트
유청종,김제한,김광우,김경화,이흥수,이문호,김경진 한국진공학회 2005 Applied Science and Convergence Technology Vol.14 No.3
We tested performance of the 4C1 beamline for analyzing structures of proteins in solution using small angle X-ray scattering (SAXS) at the Pohang Light Source(PLS). Structurally well-known proteins such as lysozyme and Bcl-XL(TM/loop) were used for the study. Low resolution solution structures of lysozyme and Bcl-XL(TM/loop) were obtained at a resolution of at least 2.2 nm, and the structures were basically same as those calculated from the crystal structures of the proteins. We also used Bcl-XL(TM/loop) with a long flexible loop attached [Bcl-XL(TM)] and obtained significantly different data from Bcl-XL(TM/loop), although the electron density map of the loop is known to be invisible from the crystal structure of Bcl-XL(TM). We confirm that SAXS experiment is a powerful tool for the structural study of proteins in solution and the 4C1 beamline at the PLS is well-equipped and suitable for the protein solution SAXS experiment. 액상 x-선 소각산란법을 이용하여 단백질의 구조를 분석하였다. 사용한 단백질은 구조가 이미 알려진 Lysozyme과 Bcl-XL(TM/loop) 그리고 Bcl-XL(TM/loop)에 자유롭게 움직이는 고리를 가진 Bcl-XL(TM)이다. Lysozyme와 Bcl-XL(TM/loop)에 대한 소각산란결과는 단백질 결정학으로부터 알려진 분자구조에서 얻은 이론적인 결과와 농도에 의한 차이정도를 제외하고는 잘 일치하였다. Bcl-XL(TM)의 경우는 단백질 결정산란 신호에서 볼 때 Bcl-XL(TM/loop)와 차이가 없는 것으로 알려져 있으나, 소각산란에서는 뚜렷한 차이를 나타내는 결과를 얻어 loop와 같이 쉽게 움직이는 부분을 가진 단백질을 연구하는 경우 소각산란의 장점을 확인할 수 있었다. 위 실험을 통하여 포항 가속기 연구소 4C1 빔라인의 성능은 적어도 해상도 ~2.2 nm까지 용액상의 단백질 구조를 분석할 수 있다는 것을 확인하였다.
용액상의 단백질 구조 분석을 위한 PLS 4Cl빔라인의 성능 테스트
유청종,김제한,김광우,김경화,이흥수,이문호,김경진,Yu Chung-Jong,Kim Jehan,Kim Kwang-Woo,Kim Ghyung-Hwa,Lee Heung-Soo,Ree Moonhor,Kim Kyung-Jin 한국진공학회 2005 Applied Science and Convergence Technology Vol.14 No.3
액상 x-선 소각산란법을 이용하여 단백질의 구조를 분석하였다. 사용한 단백질은 구조가 이미 알려진 Lysozyme과 $Bcl-XL(\vartriangle TM/\vartriangle loop)$ 그리고 $Bcl-XL(\vartriangle TM/\vartriangle loop))$에 자유롭게 움직이는 고리를 가진 $Bcl-XL(\vartriangleTM))$이다. Lysozyme와 $Bcl-XL(\vartriangle TM/\vartriangle loop)$에 대한 소각산란결과는 단백질 결정학으로부터 알려진 분자구조에서 얻은 이론적인 결과와 농도에 의한 차이정도를 제외하고는 잘 일치하였다. $Bcl-XL(\vartriangleTM))$의 경우는 단백질 결정산란 신호에서 볼 때 $Bcl-XL(\vartriangle TM/\vartriangle loop)$와 차이가 없는 것으로 알려져 있으나, 소각산란에서는 뚜렷한 차이를 나타내는 결과를 얻어 loop와 같이 쉽게 움직이는 부분을 가진 단백질을 연구하는 경우 소각산란의 장점을 확인할 수 있었다. 위 실험을 통하여 포항 가속기 연구소 4C1 빔라인의 성능은 적어도 해상도 $\sim2.2\;nm$까지 용액상의 단백질 구조를 분석할 수 있다는 것을 확인하였다. We tested performance of the 4C1 beamline for analyzing structures of proteins in solution using small angle X-ray scattering (SAXS) at the Pohang Light Source(PLS). Structurally well-known proteins such as lysozyme and $Bcl-XL(\vartriangle TM/\vartriangle loop)$ were used for the study. Low resolution solution structures of lysozyme and $Bcl-XL(\vartriangle TM/\vartriangle loop)$ were obtained at a resolution of at least i.2 nm, and the structures were basically same as those calculated from the crystal structures of the proteins. We also used $Bcl-XL(\vartriangle TM/\vartriangle loop)$ with a long flexible loop attached [$Bcl-XL(\vartriangleTM))$] and obtained significantly different data from $Bcl-XL(\vartriangle TM/\vartriangle loop)$, although the electron density map of the loop is known to be invisible from the crystal structure of $Bcl-XL(\vartriangleTM))$. We confirm that SAXS experiment is a powerful tool for the structural study of proteins in solution and the 4Cl beamline at the PLS is well-equipped and suitable for the protein solution SAXS experiment.
Study on the PAL-XFEL Beamline
이익재,유청종,구태영 한국물리학회 2007 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.51 No.I
The Pohang Accelerator Laboratory - X-ray Free Electron Laser (PAL-XFEL) beamline will provide opportunities for highly advanced experiments, such as femto-second chemistry, singleprotein scattering, and non-destructive cell imaging, at a resolution of the X-ray wavelength. It will use photons of a fundamental wavelength of 3 °A and its higher harmonics from an undulator with a fixed gap. We consider the PAL-XFEL beamline in two major parts, a front end (FE) and an experimental hall, and the beamline concept will be similar to that of the Linac Coherent Light Source (LCLS).
Magnetic Phase Study of Sr-Doped LaCoO Alloys by Using Neutron Diffraction
유영준,김재용,유청종,K.K. Yu,김기원,Y.P. Lee 한국물리학회 2006 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.49 No.III
Recent interests in strontium-doped lanthanum-cobalt oxides, LaSrCoO, have been motivated by their advanced high electrical and excellent ionic conductivity properties. These features make them good candidate materials for electrodes in fuel cells and ferroelectric memory devices where their practical applications have been hindered by technical difficulties such as fatigue and imprint. Polycrystalline La1.xSrxCoO3 (x = 0.15, 0.25 and 0.30) bulk samples were prepared by using the standard solid-state reaction. The structural properties of the samples were characterized by using X-ray diffraction and X-ray photoemission spectroscopy. By measuring the temperature dependence of the inverse magnetic susceptibility, the Curie temperatures were determined to be 147, 217, and 232 K for x = 0.15, 0.25, and 0.30 samples, respectively. The zero-field cooled magnetization measurements revealed a spin-glass like behavior for x = 0.15. Interestingly, the neutron diffraction data demonstrated little hint of an antiferromagnetic phase at low temperatures, which requires a more advanced magnetic model, including the spin state of Co, to elucidate the spin-glass behavior at low Sr concentrations.
Quantitative Coherent X-ray Diffraction Imaging of Multiple Nano Particles
김윤희,김준형,안강우,노도영,김찬,강현철,이해철,유청종 한국물리학회 2017 THE JOURNAL OF THE KOREAN PHYSICAL SOCIETY Vol.70 No.9
We report a quantitative full field electron density mapping of nano-scale objects by coherent x-ray diffractive imaging (CXDI). The projected electron density maps of two specimens, a single AuNi nanocrystal and a cluster of multi Au nanocrystals, were successfully reconstructed using CXDI. It was found that the accuracy of the electron density mapping was higher for the multiple Au nanocrystal specimen than the single AuNi particle. The improvement was attributed to the interference between the x-rays diffracted by each particle, which makes the diffraction profile complex and enhances the uniqueness of image reconstruction. The findings of this research will be useful for the quantitative analysis nano and bio systems using CXDI.