• 제목/요약/키워드: Asymmetric x-ray diffraction

검색결과 46건 처리시간 0.03초

Magnetic Properties and the Order-disorder Phase Transformation of (Fe1-XCoX) Pt Magnetic Thin Films

  • Na, K.H.;Park, C.H.;Na, J.G.;Jang, P.W.;Kim, C.S.;Lee, S.R.
    • Journal of Magnetics
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    • 제4권4호
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    • pp.119-122
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    • 1999
  • Magnetic properties and crystal structures of (Fe1-XCoX) Pt (X = 0, 0.2, 0.4, 0.5, 0.6, 0.8 and 1.0) ternary thin films were investigated. The order-disorder phase transformation of FePt thin films during annealing was also studied by x-ray diffraction and M ssbauer spectroscopy. The magnetic thin films were deposited on glass substrates using a dc sputtering method and were subsequently annealed at 400~$700^{\circ}C$ in a high vacuum. The as-deposited films exhibited a high degree of the <111> preferred orientation and the preferred orientation was not destroyed even after the subsequent post annealing. The coercivity of the ($Fe_xCo_{1-x}$) Pt thin films annealed at $700^{\circ}C$ showed a minimum value at the equiatomic composition of the Fe and Co atoms. The ordered structure of the FePt alloy was thought to have formed from the disordered structure by an inhomogeneous process, which was confirmed by the asymmetric peak shapes and M ssbauer spectra.

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Overexpression, Purification, and Preliminary X-ray Crystallographic Analysis of Human Brain-Type Creatine Kinase

  • Bong, Seung-Min;Moon, Jin-Ho;Jang, Eun-Hyuk;Lee, Ki-Seog;Chi, Young-Min
    • Journal of Microbiology and Biotechnology
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    • 제18권2호
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    • pp.295-298
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    • 2008
  • Creatine kinase (CK; E.C. 2.7.3.2) is an important enzyme that catalyzes the reversible transfer of a phosphoryl group from ATP to creatine in energy homeostasis. The brain-type cytosolic isoform of creatine kinase (BB-CK), which is found mainly in the brain and retina, is a key enzyme in brain energy metabolism, because high-energy phosphates are transfered through the creatine kinase/phosphocreatine shuttle system. The recombinant human BB-CK protein was overexpressed as a soluble form in Escherichia coli and crystallized at $22^{\circ}C$ using PEG 4000 as a precipitant. Native X-ray diffraction data were collected to $2.2{\AA}$ resolution using synchrotron radiation. The crystals belonged to the tetragonal space group $P4_32_12$, with cell parameters of a=b=97.963, $c=164.312{\AA},\;and\;{\alpha}={\beta}={\gamma}=90^{\circ}$. The asymmetric unit contained two molecules of CK, giving a crystal volume per protein mass $(V_m)$ of $1.80{\AA}^3\;Da^{-1}$ and a solvent content of 31.6%.

Crystallization and Preliminary X-ray Crystallographic Analysis of Peptide Deformylase from Staphylococcus aureus

  • Kim, Hyeon-Woo;Yoon, Hye-Jin;Kim, Hyung-Wook;Mikami, Bunzo;Suh, Se-Won
    • 한국결정학회지
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    • 제15권1호
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    • pp.40-43
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    • 2004
  • The peptide deformylase from the pathogenic bacterium Staphylococcus aureus has been over-expressed in Escherichia coli and crystallized in the presence of the inhibitor actinonin at 297 K using polyethylene glycol 20000 as a precipitant. X-ray diffraction data have been collected to 2.2 ${\AA}$ resolution. The crystal is trigonal, belonging to the space group $P3_121$ (or its enantiomorph $P3_221$), with unit cell parameters of a = b = 62.70 ${\AA}$ c = 108.23 ${\AA}$, ${\alpha}\;=\;{\beta}\;=\;90^{\circ},\;and\;{\gamma}\;=\;120^{\circ}$. An asymmetric unit contains a monomer of the recombinant enzyme, giving a $V_M$ of 2.84 ${\AA}^3\;Da^_{-1}$ and a solvent content of 56.7%.

Expression, Purification, and Crystallization of D-Psicose 3-Epimerase from Agrobacterium tumefaciens

  • Kim Kwang-Soo;Kim Hye-Jung;Oh Deok-Kun;Cheong Jong-Joo;Rhee Sang-Kee
    • Journal of Microbiology and Biotechnology
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    • 제16권4호
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    • pp.647-650
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    • 2006
  • D-Psicose 3-epimerase (DPE) catalyzes the interconversion of D-fructose to D-psicose by epimerizing the carbon-3 position. The DPE from Agrobacterium tumefaciens was cloned and expressed in Escherichia coli. The expressed enzyme was purified by affinity chromatography on an IMAC, gel filtration chromatography on a Sephacryl S-300 HR, and anion-exchange chromatography on a RESOURCE Q. The molecular mass of the purified enzyme was estimated to be about 135 kDa by Superdex 200 gel filtration chromatography, corresponding to a homotetramer. The enzyme produced crystals suitable for X-ray diffraction to a $2.0{\AA}$ resolution at 100 K. The crystals were found to belong to the orthorhombic space group $P2_12_12_1$, with unit-cell parameters a=102.4, b=113.0, and $c=131.8{\AA}$. In addition, the calculated packing parameter $(V_m)$ was $2.79{\AA}^3/Da$, the solvent content was 55.92%, and an asymmetric unit consisted of four monomers.

Crystallization and X-ray crystallographic analysis of the PH-like domain of lipid transfer protein anchored at membrane contact sites from Saccharomyces cerevisiae

  • Tong, Junsen;Im, Young Jun
    • Biodesign
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    • 제5권4호
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    • pp.136-140
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    • 2017
  • Lam6 is a member of sterol-specific ${\underline{l}ipid$ transfer proteins ${\underline{a}}nchored$ at ${\underline{m}ebrane$ contact sites (LAMs). Lam6 localizes to the ER-mitochondria contact sites by its PH-like domain and the C-terminal transmembrane helix. Here, we purified and crystallized the Lam6 PH-like domain from Saccharomyces cerevisiae. To aid crystallization of the Lam6 PH-like domain, T4 lysozyme was fused to the N-terminus of the Lam6 PH-like domain with a short dipeptide linker, GlySer. The fusion protein was crystallized under the condition of 0.1 M HEPES-HCl pH 7.0, 10% (w/v) PEG 8000, and 0.1 M $Na_3$ Citrate at 293K. X-ray diffraction data of the crystals were collected to $2.4{\AA}$ resolution using synchrotron radiation. The crystals belong to the orthorhombic space group $P2_12_12_1$ with unit cell parameters $a=59.5{\AA}$, $b=60.1{\AA}$, and $c=105.6{\AA}$. The asymmetric unit contains one T4L-Lam6 molecule with a solvent content of 58.7%. The initial attempt to solve the structure by molecular replacement using the T4 lysozyme structure was successful.

Lamp ZMR에 의한 SOI에서 비대칭 선형가열의 효과 (Effect of Asymmetric Line Heating in SOI Lamp ZMR)

  • 반효동;이시우;임인곤;주승기
    • 한국결정성장학회지
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    • 제2권2호
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    • pp.53-62
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    • 1992
  • SOI구조 형성을 위항 대용융 재결정(ZMR) 공정에서 타원형의 반사경을 기울여 빔강도분포를 인위적으로 변화시켜 실리콘 박막을 재결정시켰다. 비대칭 선형가열 효과를 해석하기 위하여 전산모사를 행하여 응고계면 근처에서의 온도분포와 열구배 변화를 조사하였다. 상부집속열원의 경사각이 증가할수록 액상의 과냉도와 실리콘 박막내의 결함열 간격은 증가하였다. 주된 결함은 연속적인 아결정립계였고 결함밀도가 낮은 경우는 isolated threading dislocations만이 관찰되었다. 단면 TEM과 박막 XRD 분석결과 실리콘 박막은 (100) 집합조직을 갖는 단결정 박막으로 재결정되었음을 확인할 수 있었다.

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Cement/PVDF hollow-fiber hybrid basement membrane: Preparation, microstructure, and separation application

  • Yabin, Zhang;Xiongfei, Du;Taotao, Zhao
    • Membrane and Water Treatment
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    • 제13권6호
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    • pp.291-301
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    • 2022
  • In this study, cement/PVDF hollow-fiber hybrid membranes were prepared via a mixed process of diffusion-induced phase separation and hydration. The presence of X-ray diffraction peaks of Ca(OH)2, an AFt phase, an AFm phase, and C-S-H phase confirmed the hydration reaction. Good hydrophilicity was obtained. The cross-sectional and surface morphologies of the hybrid membranes showed that an asymmetric pore structure was formed. Hydration products comprising parallel plates of Ca(OH)2, fibrous ettringite AFt, and granulated particles AFm were obtained gradually. For the hybrid membranes cured for different time, the pore-size distribution was similar but the porosity decreased because of blocking of the hydration products. In addition, the water flux decreased with hydration time, and carbon retention was 90% after 5 h of rejection treatment. Almost all the Zn2+ ions were adsorbed by the hybrid membrane. The above results proved that the obtained membrane could be alternative as basement membrane for separation application.

Overexpression, Crystallization, and Preliminary X-Ray Crystallographic Analysis of the Alanine Racemase from Enterococcus faecalis v583

  • Priyadarshi, Amit;Lee, Eun-Hye;Sung, Min-Woo;Kim, Jae-Hee;Ku, Min-Je;Kim, Eunice Eun-Kyeong;Hwang, Kwang-Yeon
    • Journal of Microbiology and Biotechnology
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    • 제18권1호
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    • pp.55-58
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    • 2008
  • Alanine racemase, a bacterial enzyme belonging to the fold-type III group of pyridoxal 5'-phosphate (PLP)-dependent enzymes, has been shown to catalyze the interconversion between L- and D-alanine. The alanine racemase from the pathogenic bacterium Enterococcus faecalis v583 has been overexpressed in E. coli and was shown to crystallize an enzyme at 295 K, using polyethylene glycol (PEG) 8000 as a precipitant. X-ray diffraction data to $2.5{\AA}$ has been collected using synchrotron radiation. The crystal is a member of the orthorhombic space group, $C222_1$ with unit cell parameter of a=94.634, b=156.516, $c=147.878{\AA},\;and\;{\alpha}={\beta}={\gamma}=90{\AA}$. Two or three monomers are likely to be present in the asymmetric unit, with a corresponding $V_m\; of\;3.38{\AA}^3\;Da^{-1}\;and\;2.26{\AA}^3\;Da^{-1}$ and a solvent content of 63.7% and 45.5%, respectively.

Crystallization and Preliminary X-Ray Crystallographic Analysis of UDP-N-Acetylglucosamine Enolpyruvyl Transferase from Haemophilus influenzae in Complex with UDP-N-Acetylglucosamine and Fosfomycin

  • Yoon, Hye-Jin;Ku, Min-Je;Ahn, Hyung Jun;Lee, Byung Il;Mikami, Bunzo;Suh, Se Won
    • Molecules and Cells
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    • 제19권3호
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    • pp.398-401
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    • 2005
  • The bacterial enzyme UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes the first committed step of peptidoglycan biosynthesis, i.e., transfer of enolpyruvate from phosphoenolpyruvate to UDP-N-acetyl-glucosamine. We have overexpressed the enzyme from Haemophilus influenzae in Escherichia coli and crystallized it in the apo-form, as well as in a complex with UDP-N-acetylglucosamine and fosfomycin using ammonium sulfate as the precipitant. X-ray diffraction data from a crystal of the apo-form were collected to $2.8{\AA}$ resolution at 293 K. The crystal quality was improved by co-crystallization with UDP-N-acetylglucosamine and fosfomycin. X-ray data to $2.2{\AA}$ have been collected at 100 K from a flash-frozen crystal of the complex. The complex crystals belong to the orthorhombic space group I222 (or $I2_12_12_1$) with unit-cell parameters of a = 63.7, b = 124.5, and $c=126.3{\AA}$. Assuming a monomer of the recombinant enzyme in the crystallographic asymmetric unit, the calculated Matthews parameter ($V_M$) is $2.71{\AA}^3Da^{-1}$ and solvent content is 54.6%.

비대칭 압연한 IF 강 판의 Goss 집합조직 발달 (Goss Texture Development of Asymmetrically Rolled IF Steel Sheet)

  • 김인수;남수권;김광희;이동녕
    • 소성∙가공
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    • 제26권3호
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    • pp.150-155
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    • 2017
  • To obtain the Goss texture, {110}<001>, IF steel sheets were asymmetrically rolled by 50-89% reduction in the thickness at room temperature and subsequently annealed at 200, 900, and $1200^{\circ}C$ in a box furnace under air atmosphere. The asymmetrically rolled specimens and annealed specimens show well-developed Goss texture, {110}<001>. After the IF steel sheets were asymmetrically rolled at room temperature and subsequently annealed at $900^{\circ}C$ for 1 h in a box furnace under air atmosphere, the intensity of the Goss texture, {110}<001> was high in the IF steel sheets.