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  • 1
    Electronic Resource
    Electronic Resource
    Structure-Based Inhibitors of HIV-1 Protease (1993)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 62 (1993), S. 543-585 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.62.070193.002551
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  • 2
    Electronic Resource
    Electronic Resource
    Precision of a rotating-drum film scanner (1974)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 7 (1974), S. 19-21 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Precession X-ray films were scanned with a rotating-drum microdensitometer. It is necessary to correct for non-linearity between the scanner input and output. Reliability factors for estimating the precision of scanner measurements are compared. The values of the symmetry-averaged reliability factor, Rsym, vary between 3.9 and 12% and depend strongly on the quality of films, while the values of the scanning reproducibility factor, Rrept (3.5–4%), and the film-scaling reliability factor, Rscale (4.5–5.5%), depend more on the quality of scanner software and electronics than on films.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889874008624
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  • 3
    Electronic Resource
    Electronic Resource
    The molecular symmetry of glutaminase-asparaginases: rotation function studies of the Pseudomonas 7A and Acinetobacter enzymes (1983)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 39 (1983), S. 250-257 
    Details
    ISSN: 1600-5740
    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/S0108768183002359
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  • 4
    Electronic Resource
    Electronic Resource
    Structure of insulin: results of joint neutron and X-ray refinement (1989)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 45 (1989), S. 99-107 
    Details
    ISSN: 1600-5740
    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/S0108768188011012
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  • 5
    Electronic Resource
    Electronic Resource
    Refinement of the crystal orientation matrix for the flat-cone diffractometer (1982)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 15 (1982), S. 79-81 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A procedure for refining a crystal orientation matrix for the flat-cone diffractometer is discussed. The positions of the centers of gravity of refections obtained during routine data collection are transformed in such a way that they can be used as input to the least-squares procedures of Busing & Levy [Acta Cryst. (1967), 22, 457–464] or Shoemaker & Bassi [Acta Cryst. (1970), A26, 97–101]. The orientation matrix can be refined on the basis of the positions of all observed reflections, and not only of a selected sample, thus increasing its reliability. The procedure is particularly suited for protein crystallographic studies, as it makes it possible to compensate for crystal movements encountered during data collection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889882011388
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  • 6
    Electronic Resource
    Electronic Resource
    Preliminary investigation of a new X-ray film (1981)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 14 (1981), S. 256-260 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A new X-ray film, produced by CEAVERKEN in Sweden, has recently become available. Some properties of this film have been compared to three other films commonly used in the recording of X-ray diffraction intensities (Agfa T4, Kodak No-screen, Ilford Industrial G). The linearity of CEA film has been found to be similar to that for Agfa and Ilford. The speed of the new film is about 10% lower than Agfa or Kodak, and the film factor was measured to be 2.9 for Cu Kα radiation. The background level is significantly lower than on the other three films investigated. This combination of properties makes CEA film suitable for routine collection of X-ray diffraction data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S002188988100931X
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  • 7
    Electronic Resource
    Electronic Resource
    Absorption correction for Weissenberg diffractometers (1980)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 36 (1980), S. 442-450 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Formulas are derived extending several semi-empirical absorption-correction methods to diffractometers operating in Weissenberg geometries, with particular attention paid to flat-cone geometry. These formulas are useful for a variety of instruments using both area and linear position-sensitive detectors. While a complete data set can sometimes be corrected using a single absorption reflection, it was found that the best corrections are usually obtained by considering two absorption reflections rather than one. A discussion of the optimum choice of absorption correction when a crystal has at least a twofold symmetry axis is presented. The accuracy of the methods and the limits of applicability have been examined by computer simulations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739480000952
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  • 8
    Electronic Resource
    Electronic Resource
    A procedure for joint refinement of macromolecular structures with X-ray and neutron diffraction data from single crystals (1982)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 38 (1982), S. 239-247 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A procedure is presented for the stereochemically restrained least-squares refinement of macromolecular structures with neutron and X-ray diffraction data from single crystals. This procedure has been tested by refining a model of ribonuclease A using neutron data to minimal spacings of 2.8 Å and X-ray data from within 2.0 Å spacings. Joint X-ray and neutron refinement is well conditioned and tends to avoid false minima that may occur when a medium-resolution structure is refined solely with the neutron structure factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739482000527
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  • 9
    Electronic Resource
    Electronic Resource
    A Minimalist's Approach to the Phase Problem – Phasing Selenomethionyl Protein Structures Using Cu Kα Data (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1075-1081 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The feasibility of phasing protein structures through the use of the isomorphous and anomalous signal of selenomethionyl (Se-Met) derivative and diffraction data collected with a standard laboratory Cu Kα X-ray source has been investigated. Interpretable electron-density maps were obtained for the core domain of avian sarcoma virus integrase, a typical medium-sized protein having four Met residues in a sequence of 156 amino acids. The r.m.s. difference between 3.1 Å experimental phases obtained from Se-Met Cu Kα data and the final phases calculated from the refined model is 55°. A procedure combining single isomorphous replacement/single anomalous scattering phasing and solvent flattening for data based on a single Se-Met derivative and Cu Kα radiation has been tested on this and another protein. The results are encouraging enough to indicate that such procedures might be recommended when a synchrotron source is not readily available.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996008402
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  • 10
    Electronic Resource
    Electronic Resource
    Refined crystal structure of Acinetobacter glutaminasificans glutaminase–asparaginase (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 826-832 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of glutaminase–asparaginase from Acinetobacter glutaminasificans has been reinterpreted and refined to an R factor of 0.171 at 2.9 Å resolution, using the same X-ray diffraction data that were used to build a preliminary model of this enzyme [Ammon, Weber, Wlodawer, Harrison, Gilliland, Murphy, Sjölin & Roberts (1988). J. Biol. Chem. 263, 150–156]. The current model, which does not include solvent, is based in part on the related structure of Escherichia coli asparaginase and is significantly different from the structure of the enzyme from A. glutaminasificans described previously. The reason for the discrepancies has been traced to insufficient phasing power of the original heavy-atom derivative data, which could not be compensated for fully by electron-density modification techniques. The corrected structure of A. glutaminasificans glutaminase–asparaginase is presented and compared with the preliminary model and with the structure of E. coli asparaginase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994003446
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