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Kim, Hyunuk,Samsonenko, Denis G.,Das, Sunirban,Kim, Ghyung-Hwa,Lee, Heung-Soo,Dybtsev, Danil N.,Berdonosova, Elena A.,Kim, Kimoon Wiley (John WileySons) 2009 Chemistry - An Asian Journal Vol.4 No.6
<P>Sorption isotherms of methane in Zn(2)(bdc)(2)(dabco) are measured up to a pressure of 35 bar in the temperature range between 198-296 K. The methane sorption measurements at 296 K showed an uptake of 137 cm(3) cm(-3) at 35 bar. The enthalpy of methane adsorption for Zn(2)(bdc)(2)(dabco) estimated by the virial equation is 13.6 kJ mol(-1) at zero coverage. X-ray structure analysis of methane-adsorbed Zn(2)(bdc)(2)(dabco) by synchrotron radiation at 90 K revealed that methane molecules occupy three independent sorption sites (A, B, and C) with a stoichiometry of Zn(2)(bdc)(2)(dabco) x 6.69 CH(4), which is consistent with the results of the gas sorption measurements at 198 K. In a cavity, eight symmetry-related methane sorption sites A are located near the {Zn(2)(CO(2))(4)} paddle-wheel units, while four symmetry-related methane sorption sites B are near the center of the small windows along the a and b axes. Both A and B sites are half-occupied. Methane molecules occupying sites A are not only in van der Waals contact with the paddle-wheel units, but also interact with the phenyl rings of bdc ligands through partial pi-HC interactions. Methane molecules in B sites interact with the side of the phenyl rings through van der Waals interaction. The site C, located at the center of the cavity, is a secondary sorption site; methane molecules occupying sites C are in van der Waals contact with those in sites A and B.</P>
Crystal structure of Escherichia coli MazG, the regulator of nutritional stress response.
Lee, Sujin,Kim, Myung Hee,Kang, Beom Sik,Kim, Jeong-Sun,Kim, Ghyung-Hwa,Kim, Yeon-Gil,Kim, Kyung Jin American Society for Biochemistry and Molecular Bi 2008 The Journal of biological chemistry Vol.283 No.22
<P>MazG is a nucleoside triphosphate pyrophosphohydrolase that hydrolyzes all canonical nucleoside triphosphates. The mazG gene located downstream from the chromosomal mazEF 'addiction module,' that mediated programmed cell death in Escherichia coli. MazG activity is inhibited by the MazEF complex both in vivo and in vitro. Enzymatic activity of MazG in vivo affects the cellular level of guanosine 3',5'-bispyrophosphate (ppGpp), synthesized by RelA under amino acid starvation. The reduction of ppGpp, caused by MazG, may extend the period of cell survival under nutritional stress. Here we describe the first crystal structure of active MazG from E. coli, which is composed of two similarly folded globular domains in tandem. Among the two putative catalytic domains, only the C-terminal domain has well ordered active sites and exhibits an NTPase activity. The MazG-ATP complex structure and subsequent mutagenesis studies explain the peculiar active site environment accommodating all eight canonical NTPs as substrates. In vivo nutrient starvation experiments show that the C terminus NTPase activity is responsible for the regulation of bacterial cell survival under nutritional stress.</P>
Park, Young Kwan,Choi, Sang Beom,Kim, Hyunuk,Kim, Kimoon,Won, Byoung-Ho,Choi, Kihang,Choi, Jung-Sik,Ahn, Wha-Seung,Won, Nayoun,Kim, Sungjee,Jung, Dong Hyun,Choi, Seung-Hoon,Kim, Ghyung-Hwa,Cha, Sun-Sh WILEY-VCH Verlag 2007 Angewandte Chemie Vol.119 No.43
<B>Graphic Abstract</B> <P>Poren zeigen Größe: Ein mesoporöses metall-organisches Netzwerk, das vorrangig aus Tb<SUP>3+</SUP>-Ionen und tripodalen Carboxylatliganden aufgebaut ist, bringt es auf Käfige mit 3.9 und 4.7 nm Durchmesser (siehe Bild). Das leere Netzwerk ist beständig und kann Gas- oder Ferrocenmoleküle aufnehmen, was durch Gassorptions- und Lumineszenzstudien bestätigt wurde. <img src='wiley_img/00448249-2007-119-43-ANGE200702324-content.gif' alt='wiley_img/00448249-2007-119-43-ANGE200702324-content'> </P>
Park, Young Kwan,Choi, Sang Beom,Kim, Hyunuk,Kim, Kimoon,Won, Byoung-Ho,Choi, Kihang,Choi, Jung-Sik,Ahn, Wha-Seung,Won, Nayoun,Kim, Sungjee,Jung, Dong Hyun,Choi, Seung-Hoon,Kim, Ghyung-Hwa,Cha, Sun-Sh WILEY-VCH Verlag 2007 Angewandte Chemie. international edition Vol.46 No.43
<B>Graphic Abstract</B> <P>Supersized pores: A new mesoporous metal–organic framework that is mainly composed of Tb<SUP>3+</SUP> ions and tripodal carboxylate ligands has cages of 3.9 and 4.7 nm in diameter (see picture). The evacuated framework is robust and can accommodate gases or ferrocene molecules, as verified by gas-sorption measurements and luminescence studies. <img src='wiley_img/14337851-2007-46-43-ANIE200702324-content.gif' alt='wiley_img/14337851-2007-46-43-ANIE200702324-content'> </P>
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.
Synthesis and Crystal Structure of Lead Iodide in the Sodalite Cavities of Zeolite A (LTA)
Kim, Seok-Han,Lim, Woo-Taik,Kim, Ghyung-Hwa,Lee, Heung-Soo,Heo, Nam-Ho Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.5
The positions of $PbI _2$ molecule synthesized into the molecular-dimensioned cavities of $\mid K_6 (Pb _4I_2)(PbI_2) _{0.67}-(H_2O)_2\mid [Si _{12}Al _{12}O _{48}]$-LTA have been determined. A single crystal of $\mid Pb _6\mid [Si _{12}Al _{12}O _{48}]$-LTA, prepared by the dynamic ion-exchange of $\mid Na _{12}\mid [Si _{12}Al _{12}O _{48}]$-LTA with aqueous 0.05 M $Pb _(NO _3)_2$ and washed with deionized water, was placed in a stream of flowing aqueous 0.05 M KI at 294 K for three days. The resulting crystal structure of the product $( \mid K_6 (Pb _4I_2)(PbI_2) _{0.67}(H_2O)_2\mid [Si _{12}Al _{12}O _{48}]$-LTA, a = 12.353(1) $\AA$) was determined at 294 K by single-crystal X-ray diffraction in the space group Pm3 m. It was refined with all measured reflections to the final error index $R_1$ = 0.062 for 623 reflections which $F_o$ > 4$\sigma$($F_o$). 4.67 $Pb ^{2+}$ and six $K^+$ ions per unit cell are found at three crystallographically distinct positions: 3.67 $Pb ^{2+}$ and three $K^+$ ions on the 3-fold axes opposite six-rings in the large cavity, three $K^+$ ions off the plane of the eight-rings, and the remaining one $Pb ^{2+}$ ion lies opposite four-ring in the large cavity. 0.67 $Pb ^{2+}$ ions and 1.34 $I^-$ ions per unit cell are found in the sodalite units, indicating the formation of a $PbI _2$ molecule in 67% of the sodalite units. Each $PbI _2$ (Pb-I = 3.392(7) $\AA$) is held in place by the coordination of its one $Pb ^{2+}$ ion to the zeolite framework (a $Pb ^{2+}$ cation is 0.74 $\AA$ from a six-ring oxygens) and by the coordination of its two $I^-$ ions to $K^+$ ions through six-rings (I-K = 3.63(4) $\AA$). Two additional $I^-$ ions per unit cell are found opposite a four-ring in the large cavity and form $Pb _2K_2I^{5+}$ and $Pb _2K_2I^{3+}$ moieties, respectively, and two water molecules per unit cell are also found on the 3-fold axes in the large cavity.