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  • 1
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    Need for neutron diffraction instruments (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langan, P -- Schoenborn, B P -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1089.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610521" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography/*instrumentation ; *Neutrons ; Proteins/*chemistry ; United States
    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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    A complete mapping of the proteins in the small ribosomal subunit of Escherichia coli (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-04
    Description: The relative positions of the centers of mass of the 21 proteins of the 30S ribosomal subunit from Escherichia coli have been determined by triangulation using neutron scattering data. The resulting map of the quaternary structure of the small ribosomal subunit is presented, and comparisons are made with structural data from other sources.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Capel, M S -- Engelman, D M -- Freeborn, B R -- Kjeldgaard, M -- Langer, J A -- Ramakrishnan, V -- Schindler, D G -- Schneider, D K -- Schoenborn, B P -- Sillers, I Y -- AI-09167/AI/NIAID NIH HHS/ -- AI-20466/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Brookhaven National Laboratory, Upton, NY 11973.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317832" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*analysis ; Escherichia coli/*ultrastructure ; Models, Structural ; Neutrons ; Ribosomal Proteins/*analysis ; Ribosomes/*ultrastructure
    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
    The crystal structure of the monoterpene iridomyrmecin at –150°C (1964)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 17 (1964), S. 472-477 
    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/S0365110X64001153
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    A neutron Fourier chopper for single crystal reflectivity measurements: some general design considerations (1971)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 27 (1971), S. 284-291 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Neutron single-crystal analysis of complex protein structures requires the collection of intensity data on a large number of reflections. The use of time-of-flight analysis (in particular Fourier time-of-flight analysis employing phase detection) of diffraction data, offers a significant increase in the efficiency of the use of reactor neutrons. Such a method would facilitate the use of neutron diffraction in protein structure work. In this paper, we investigate the use of the Fourier chopper in single-crystal work. We examine the effect of various system parameters (frequency stability, flight path fluctuations, collimation, sample mosaic spread, inaccuracy in phase detection, and statistical counting errors) and determine general specifications for such an apparatus. None of these specifications appears to be beyond present day technology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739471000640
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  • 5
    Electronic Resource
    Electronic Resource
    Multilayer neutron monochromators (1977)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 33 (1977), S. 805-813 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Thin-film multilayer monochromators have been fabricated and studied by neutron diffraction. Alternating thin films of two materials, such as Mn and Ge, constitute a one-dimensional crystal owing to the contrast in their scattering amplitude densities. The following are novel features of such a monochromator: (1) large and adjustable d spacing, (2) very high reflectivity, (3) adjustable bandwidth, Δλ/λ. Both kinematical and dynamical theories have been developed to give a proper understanding of the properties of a multilayer. Since a deviation from perfect periodicity can have a substantial effect on diffraction properties of a multilayer, a 'disorder factor' has been introduced in the dynamical theory. Finite resolution of the spectrometer has been taken into consideration when the experimental data are compared with the theoretical expressions. These multilayers can also be used as excellent polarizers and filters for neutrons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S056773947700196X
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  • 6
    Electronic Resource
    Electronic Resource
    A Low-Resolution Low-Temperature Neutron Diffraction Study of Myoglobin (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 544-550 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Diffraction data to 5 Å resolution were collected on a myoglobin crystal at 80, 130, 180 and 240 K. The linear coefficient of thermal expansion for myoglobin was determined to be 45 × 10−6 K−1, based on the measured expansion of the unit-cell parameters. The nature of the hydration layers surrounding the protein in the crystal is described in terms of a shell solvent model, which was used to calculate the coefficient of thermal expansion in reasonable agreement with the measured value. Wilson statistics were calculated and discussed in terms of an averaged disorder model. [F(T2) − F(80 K) exp(−iφ)] Fourier maps were calculated where T2 was taken as 130, 180 and 240 K, respectively. None of these difference maps showed any features above 2.0σ in the protein region. The 130 and 240 K difference maps showed many small and widely distributed negative difference features and showed very few positive difference features above 2.5σ in the solvent region. However, the 180 K difference map showed an extensive negative difference feature at the interface between symmetry-related molecules, occurring in the vicinity of residues 40-50 on one molecule and 76-80 on a symmetry-related molecule. These difference neutron Fourier maps indicate a concerted effect at 180 K, which is interpreted in terms of an onset of extended lattice disorder.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997004356
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  • 7
    Electronic Resource
    Electronic Resource
    Peak-shape analysis for protein neutron crystallography with position-sensitive detectors (1983)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 39 (1983), S. 315-321 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: In neutron protein crystallography, the use of position-sensitive detectors controlled by a modern data acquisition system permits new approaches to data collection strategies. Instead of dealing with conventional scans, like the θ-2θ scan, that provide an integrated intensity as a function of a rotational parameter, the computer-linked counter can be used to produce a three-dimensional reflection profile. As the crystal steps (Δω) through a reflection, the observed data for each step are stored in an external memory as a function of extent in 2θ and height (y) of a reflection. In this space, the reflection will be a three-dimensional distribution with dimensions determined by such basic geometrical conditions as Δλ, crystal size, mosaic spread, counter-resolution, and beam-collimation parameters. Knowledge of the interaction of these basic parameters will allow the design of optimal beam optics and will permit the delineation of the reflection from the background and permit, therefore, an accurate intensity determination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108767383000732
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  • 8
    Electronic Resource
    Electronic Resource
    Correction factors for neutron diffraction from lamellar structures (1977)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 33 (1977), S. 813-818 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: In a spectrometer with finite beam divergence the vertical size of the reflections will increase with the order of reflection. This effect will be more pronounced if the mosaic width of the sample is large, which is often the case with biological samples. When the size of the reflection is greater than the detector size, a correction factor has to be introduced to account for this loss of intensity. A method of calculating this correction factor for a given beam divergence and mosaic width has been developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739477001971
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  • 9
    Electronic Resource
    Electronic Resource
    Neutron Scattering (1972)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 1 (1972), S. 529-552 
    Details
    ISSN: 0084-6589
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bb.01.060172.002525
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  • 10
    Electronic Resource
    Electronic Resource
    Binding of Xenon to Horse Haemoglobin (1965)
    [s.l.] : Nature Publishing Group
    Nature 208 (1965), S. 760-762 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THIS article is a sequel to the recent report on the A binding of xenon to sperm whale myoglobin1. There it was shown by an X-ray diffraction analysis that a single atom of xenon binds to a specific site buried in the interior of myoglobin, in contact with one of the pyrrole rings of the haem ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/208760a0
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