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  • 1
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    The catalytic pathway of cytochrome p450cam at atomic resolution (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlichting, I -- Berendzen, J -- Chu, K -- Stock, A M -- Maves, S A -- Benson, D E -- Sweet, R M -- Ringe, D -- Petsko, G A -- Sligar, S G -- GM31756/GM/NIGMS NIH HHS/ -- GM33775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1615-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Molecular Physiology, Department of Physical Biochemistry, Otto Hahn Strasse 11, 44227 Dortmund, Germany. ilme.schlichting@mpi-dortmund.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698731" target="_blank"〉PubMed〈/a〉
    Keywords: Camphor/*chemistry/*metabolism ; Camphor 5-Monooxygenase/*chemistry/*metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Electrons ; Ferric Compounds/chemistry/metabolism ; Ferrous Compounds/chemistry/metabolism ; Hydrogen Bonding ; Hydroxylation ; Ligands ; Models, Molecular ; Molecular Conformation ; Oxygen/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protons ; Pseudomonas putida/enzymology ; Water/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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    Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bolduc, J M -- Dyer, D H -- Scott, W G -- Singer, P -- Sweet, R M -- Koshland, D E Jr -- Stoddard, B L -- GM49857/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1312-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Program in Structural Biology, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761851" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Computer Graphics ; *Crystallography, X-Ray ; Isocitrate Dehydrogenase/*chemistry/genetics/metabolism ; Isocitrates/metabolism ; Kinetics ; *Mutagenesis, Site-Directed ; NADP/metabolism ; Protein Conformation
    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
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    Response (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, P T -- Smalds, A -- Carty, R P -- Mangel, W F -- Sweet, R M -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):621-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17758171" target="_blank"〉PubMed〈/a〉
    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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  • 4
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    The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: Crystals of bovine trypsin were acylated at the reactive residue, serine 195, to form the transiently stable p-guanidinobenzoate. Hydrolysis of this species was triggered in the crystals by a jump in pH. The hydrolysis was monitored by three-dimensional Laue crystallography, resulting in three x-ray diffraction structures, all from the same crystal and each representing approximately 5 seconds of x-ray exposure. The structures were analyzed at a nominal resolution of 1.8 angstroms and were of sufficient quality to reproduce subtle features in the electron-density maps for each of the structures. Comparison of the structures before and after the pH jump reveals that a water molecule has positioned itself to attack the acyl group in the initial step of the hydrolysis of this transient intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, P T -- Smalas, A -- Carty, R P -- Mangel, W F -- Sweet, R M -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):669-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Argonne National Laboratory, IL 60439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Crystallography/methods ; Indicators and Reagents ; Models, Molecular ; *Protein Conformation ; Serine ; Trypsin/*chemistry ; Water
    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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  • 5
    Electronic Resource
    Electronic Resource
    Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution (1974)
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 4212-4228 
    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/bi00717a024
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  • 6
    Electronic Resource
    Electronic Resource
    Consideration in the choice of a wavelength range for white-beam Laue diffraction (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 49 (1993), S. 305-307 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The white-beam Laue-diffraction method is a useful tool for rapid measurement of crystallographic intensities with synchrotron radiation. Considerations of the signal-to-noise ratio to be expected from scattering of X-rays within a limited wavelength range suggest that it will pay to limit that range to something like an octave. This rule-of-thumb has the added advantage that there will be significantly fewer diffraction spots that are overlapping harmonics of one another. To maximize the number of reflections recorded in a single stationary-crystal exposure, one should choose this octave of wavelengths in a region where the curvature of the Ewald sphere is greatest, that is at the longest wavelength allowable after other considerations are taken into account.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444992012095
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  • 7
    Electronic Resource
    Electronic Resource
    Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 197-201 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: We report the crystallization of samples of a recombinant preparation of human interleukin-1 receptor antagonist protein (IRAP) and solution of the crystal structure by isomorphous replacement methods. Crystals were obtained by the hanging-drop vapor-diffusion method at 277 K from solutions of PEG 4000 containing sodium chloride, dithiothreitol and PIPES [sodium piperazione-N,N′-bis(2-ethanesulfonate)] buffer at pH 7.0. Crystals appear within about a week and grow as truncated tetragonal bipyramids to 0.3–0.6 mm on an edge. X-ray diffraction data from these crystals specify space group P43212 and unit-cell dimensions of a = b = 72.35(26), c = 114.7(8) Å and Z = 16 (two molecules per asymmetric unit). Fresh crystals diffract to about 2.3 Å resolution. The search for heavy-atom derivatives has produced two, potassium gold cyanide and trimethyl lead chloride, as same-site, single-site derivatives. Inspection of an electron-density map at 4 Å resolution calculated with these derivatives confirms that the IRAP molecule is a member of the interleukin-1 structural family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993009394
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  • 8
    Electronic Resource
    Electronic Resource
    Treatment of diffraction data from crystals twinned by merohedry (1980)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 36 (1980), S. 755-760 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of the protein B-phycoerythrin from the red alga Porphyridium cruentum undergo twinning by merohedry in which the two members of the twin are related by rotation about (1,1,-1,0), a symmetry operation of the lattice but not of the crystals. Several methods are compared for estimation of the volume fractions of the two members of the twin so that measured data can be corrected for this twinning. The effect of these corrections on the final electron-density map is analyzed. Results show that when the volume fraction of the smaller crystal in a twinned specimen used for structure determination by multiple isomorphous replacement is 0-0.1, correction of diffraction data for twinning results in a small but significant improvement in the accuracy of the electron- density map.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739480001520
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  • 9
    Electronic Resource
    Electronic Resource
    The crystal and molecular structure of purine (1965)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 19 (1965), S. 573-580 
    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/S0365110X65003900
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  • 10
    Electronic Resource
    Electronic Resource
    Treatment of diffraction data from protein crystals twinned by merohedry: erratum (1981)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 37 (1981), S. 137-137 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A printer's error has occurred in Fisher & Sweet [Acta Cryst. (1980), A36, 755-780]. Seven lines from the bottom of the left-hand column of page 755 a bar has been omitted from khi\bar l. The sentence should read: Although distinct twin domains can sometimes be distinguished in the polarizing microscope, the twinning is of the twin-lattice-symmetry type (Donnay & Donnay, 1974) in which reflection hkil of crystal I is superimposed onto reflection khi\bar l of crystal II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739481000260
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