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  • 1
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    Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: The crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L -- Durley, R C -- Mathews, F S -- Davidson, V L -- GM41574/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):86-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140419" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/metabolism ; Computer Graphics ; Cytochrome c Group/*chemistry/metabolism ; Electron Transport ; Hydrogen Bonding ; *Indolequinones ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/metabolism ; Paracoccus denitrificans/*chemistry/enzymology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Quinones/chemistry/metabolism ; Software ; Tryptophan/analogs & derivatives/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Z W -- Koh, M -- Van Driessche, G -- Van Beeumen, J J -- Bartsch, R G -- Meyer, T E -- Cusanovich, M A -- Mathews, F S -- GM-20530/GM/NIGMS NIH HHS/ -- GM-21277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):430-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939681" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chromatium/*enzymology ; Computer Graphics ; Crystallography, X-Ray ; Cytochrome c Group/*chemistry ; Electron Transport ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Models, Molecular ; Oxidoreductases/*chemistry ; Protein Conformation ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    Electron Tunneling in Substrate-Reduced Trimethylamine Dehydrogenase: Kinetics of Electron Transfer and Analysis of the Tunneling Pathway (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 2584-2591 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00008a024
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  • 4
    Electronic Resource
    Electronic Resource
    Rotation-function study of flavocytochrome b2 (1979)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 35 (1979), S. 412-416 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A rotation-function study of flavocytochrome b2 has been carried out using X-ray data from crystals which contain one tetramer of 230 000 Dalton per asymmetric unit. The function computed from 10-5.5 Å resolution data clearly shows the orientation of the molecular 222 symmetry axes. The presence of these symmetry elements is consistent with previous structural and biochemical studies of the molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739479001005
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  • 5
    Electronic Resource
    Electronic Resource
    A microprocessor-controlled optical incremental angle encoder system for the Picker FACS-I diffractometer (1979)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 12 (1979), S. 425-425 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889879012917
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  • 6
    Electronic Resource
    Electronic Resource
    Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution : (I) X-ray Analysis (1968)
    [s.l.] : Nature Publishing Group
    Nature 219 (1968), S. 29-32 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The phase angles of 8,000 reflexions were determined by the method of isomorphous replacement, using crystals of native haemoglobin and of three heavy atom derivatives. The electron density maps show the positions of nearly all the amino-acid residues and some details of the haem groups. Next week ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/219029a0
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  • 7
    Electronic Resource
    Electronic Resource
    Refinement and structural analysis of bovine cytochrome b5 at 1.5 Å Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 65-76 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of bovine liver cytochrome b5, a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 Å resolution, has been refined at 1.5 Å using data collected on a diffractometer. Refinement to 2.0 Å resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 Å resolution using the program PROFFT. Only residues 3–87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5–5 Å. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995007827
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  • 8
    Electronic Resource
    Electronic Resource
    The molecular and crystal structure of (BH2)3[N(CH3)2]3 (1961)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 14 (1961), S. 273-278 
    Details
    ISSN: 0001-5520
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0365110X61000851
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  • 9
    Electronic Resource
    Electronic Resource
    X-ray Structure of the Cupredoxin Amicyanin, from Paracoccus denitrificans, Refined at 1.31 Å Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 676-686 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: High-resolution X-ray diffraction data to dmin = 1.31 Å were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 Å structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0–1.3 Å. Comparison of the 1.31 Å structure with that at 2.0 Å shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996001072
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  • 10
    Electronic Resource
    Electronic Resource
    A semi-empirical method of absorption correction (1968)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 24 (1968), S. 351-359 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: An extension of Furnas's method is described. The variation of intensity of an axial reflection as the crystal is rotated about the goniometer axis is used to give a curve of relative transmission T against azimuthal angle φ for the corresponding reciprocal lattice level. Transmission coefficients for any general reflexion hkl are then given approximately by T(hkl) = [T(φinc) + T(φret)]/2 where φinc and φret are the azimuthal angles of the incident and reflected beams. Equations are derived for (φinc and φret and the accuracy of the method is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739468000707
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