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  • International Union of Crystallography (IUCr)  (3)
  • American Institute of Physics (AIP)  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Methyl group dynamics in the crystalline alanine dipeptide: A combined computer simulation and inelastic neutron scattering analysis (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 8864-8879 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The dynamics of the methyl groups in the crystalline alanine dipeptide is examined over a wide range of temperatures using elastic and inelastic neutron scattering experiments and molecular dynamics (MD) simulations of the full crystal. Neutron scattering spectra are calculated from the simulations and directly compared to the experimental profiles. The N-ter and C-ter methyl groups in the molecule have low rotational barriers, i.e., (approximately-less-than)1 kcal/mol. They undergo rotations that are activated on time scales faster than ≈1 ns at temperatures as low as 50–100 K and are on the picosecond time scale at 150 and 300 K. At 300 K the rotational motion becomes strongly diffusive in the simulation. In contrast, the side-chain methyls possess a significant intramolecular intrinsic torsional barrier, ≈3 kcal/mol. As a result, their dynamics consists of librations and rare jumps between wells. The simulations are further analyzed to characterize in detail the motions giving rise to the calculated scattering. Using a quaternion-based method the simulated methyl dynamics is decomposed into rigid-body rotational and translational components. The decomposed motions and their contributions to the calculated neutron profiles are examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.463361
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  • 2
    Electronic Resource
    Electronic Resource
    Interconversion of Crystals of the Escherichia coli EF-Tu (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 799-805 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of the complex formed between the two bacterial polypeptide elongation factors, EF-Tu and EF-Ts, produced from solutions of PEG 6000 can be of two morphologically similar forms both of space group P212121. One form diffracts to only about 3 Å resolution, the other to better than 2.4 Å resolution. These forms can be interconverted and the transformation of one into the other has been shown to be solely a result of dehydration/hydration processes. By designing a suitable soaking protocol and careful control of the experimental parameters for data collection at cryotemperatures, complete data sets for the high-resolution form could be obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996002259
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  • 3
    Electronic Resource
    Electronic Resource
    Preliminary X-ray diffraction studies on asparaginyl-tRNA synthetase from Thermus thermophilus (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 195-196 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The recombinant asparginyl-tRNA synthetase from the thermophilic bacterium Thermus thermophilus expressed in Escherichia coli has been crystallized from PEG 6000 solutions. Depending on the PEG concentrations the crystals were in either tetragonal or hexagonal space groups. Although generally smaller, the latter (space group P6422) diffracted better, to a resolution of 2.8 Å. Using the coordinates of the yeast aspartyl-tRNA synthetase structure molecular replacement methods were applied to both tetragonal and hexagonal crystals; a solution was found which gave excellent crystal packing in both space groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996014096
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  • 4
    Electronic Resource
    Electronic Resource
    Preliminary X-ray diffraction studies on asparaginyl-tRNA synthetase from Thermus thermophilus. Erratum (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 491-491 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997099198
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