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  • 1
    Electronic Resource
    Electronic Resource
    The [(4 + 2) + (3 + 2)] route to multiply fused ring systems: a new notion in polycycle construction (1984)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 106 (1984), S. 1845-1847 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00318a054
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  • 2
    Electronic Resource
    Electronic Resource
    Cathodic Action of the Uranyl-Itaconate Complex at the Dropping Mercury Electrode. (1964)
    s.l. : American Chemical Society
    Analytical chemistry 36 (1964), S. 26-28 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60207a013
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  • 3
    Electronic Resource
    Electronic Resource
    Preparation and X-ray crystallographic analysis of recombinant obelin crystals diffracting to beyond 1.1 Å (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1919-1921 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of recombinant obelin, the Ca2+-regulated photoprotein from the marine hydroid Obelia longissima, have been grown from a solution containing PEG 8000 and potassium phosphate. Hexaminecobalt trichloride was used as an additive to increase the chance of crystallization. The crystals grow in a light yellow cubic form (0.5 × 0.5 × 0.45 mm) which diffracts to beyond 1.1 Å resolution. The crystals belong to the space group C2, with unit-cell parameters a = 83.43, b = 54.92, c = 52.99 Å, β = 112.00°. The asymmetric unit contains one molecule. Crystals exposed to calcium ion before and after X-ray irradiation emit light, confirming that the crystals consist of an active photoprotein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901016523
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  • 4
    Electronic Resource
    Electronic Resource
    Preparation and preliminary study of crystals of the recombinant calcium-regulated photoprotein obelin from the bioluminescent hydroid Obelia longissima (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1965-1966 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of recombinant obelin, the Ca2+-regulated photoprotein from the marine hydroid Obelia longissima, have been grown from sodium citrate solutions. Crystals grow as hexagonal light-yellow rods (0.1 × 0.1 × 1.0 mm) which diffract to beyond 1.8 Å with synchrotron radiation of 1.0 Å wavelength. The crystals have a primitive hexagonal lattice with unit-cell parameters a = 81.55, c = 86.95 Å. The asymmetric unit contains two molecules. This represents the successful preparation of single crystals of a photoprotein obelin which have promising diffraction properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999011828
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  • 5
    Electronic Resource
    Electronic Resource
    New crystal forms of a μ-class glutathione S-transferase from rat liver (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 219-224 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Two new crystal forms of isoenzyme 3-3 of rat liver glutathione S-transferase (GST 3-3) have been obtained. They were grown under essentially the same crystallization conditions as those reported for the C2 crystal form [Fu, Rose, Chung, Tam & Wang (1991). Acta Cryst. B47, 813–814]. The new crystals belong to space group P21 with one form having cell dimensions a = 101.6, b = 69.5, c = 81.4 Å, and β = 113.6°, and the other form having cell parameters a = 97.4, b = 81.1, c = 69.4 Å and β = 109.2°. These new crystals diffract to at least 2.5 Å, resolution. The molecular packing arrangements in these P21 crystals have been found by molecular replacement studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993009370
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  • 6
    Electronic Resource
    Electronic Resource
    Improved crystals of the toxic protein MAP by protein engineering towards the host specificity (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 404-407 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Mirabilis anti-viral protein (MAP) is a ribosome-inactivating protein from Mirabilis jalapa L. Since MAP is effective over a broad spectrum of species, the protein is difficult to express in heterologous hosts such as Escherichia coli. Recently, we obtained a MAP mutant, Y72F which exhibits a lower (1/100) activity against E. coli ribosomes while retaining almost full activity against mammalian cells [Habuka, Miyano, Kataoka, Tsuge & Noma (1992). J. Biol. Chem. 267, 7758–7760]. For the crystallographic studies, the Y72F MAP expression vector with an OmpA leading sequence was constructed and expressed in E. coli. The Y72F MAP mutant was then isolated and purified from the cell culture medium. Crystals were grown using the crystallization conditions for the native MAP crystals [Miyano et al. (1992). J. Mol. Biol. 226, 281–283]: 50% ammonium sulfate containing 50 mM ammonium citrate and 2 mM adenine sulfate, pH 5.4. The crystals belong to space group P3121 (or P3221) with a = b = 104.1 and c = 134.3 Å. The crystals are isomorphous with the wild-type crystals but diffract to higher resolution. Imaging-plate photographs of the Y72F mutant showed sharp intense spots without the streaking observed in the native crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994002325
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary crystallographic data for the augmenter of liver regeneration (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 331-334 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A new cellular growth factor termed augmenter of liver regeneration (ALR) has been crystallized. ALR has been shown to have a proliferative effect on liver cells while at the same time producing an immunosuppressive effect on liver-resident natural killer cells and liver-resident mononuclear leukocytes. In addition, ALR appears to play an important role in the synthesis and stabilization of mitochondrial gene transcripts in actively regenerating cells. ALR crystals diffract to beyond 2 Å resolution and belong to space group P21212, with a = 125.1, b = 108.1 and c = 38.5 Å. Based on four molecules per asymmetric unit, the Matthews coefficient is calculated to be 2.16 Å3 Da−1 which corresponds to a solvent content of 43%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996014084
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  • 8
    Electronic Resource
    Electronic Resource
    Angle settings for rotation around the diffraction vector for four-circle diffractometers (1976)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 32 (1976), S. 918-919 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Simple graphical representations have been found which have led to the discovery of new geometrical relations between the angle settings, χ0, ω, χ and φ-φ0, of a four-circle single-crystal diffractometer, and the azimuthal angle, ψ, of the diffraction vector. The new geometric relations greatly simplify the derivation of the trigonometric equations which relate the angle settings with the rotation around the diffraction vector. One of these equations, tan χ = tan χ0/cos (φ - φ0), is given here for the first time. The others are similar in form to those derived previously with matrix methods.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739476001848
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  • 9
    Electronic Resource
    Electronic Resource
    Crystals of Ligand-Free Bovine Neurophysin II (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 946-949 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A modified neurophysin, des 1-6 bovine neurophysin II, has been crystallized in the absence of bound hormone or hormone analogue. These crystals represent the first crystals of ligand-free neurophysin, and are essential for understanding neurophysin–hormone recognition as well as hormone-induced neurophysin dimerization. The crystals diffract to beyond 1.8 Å resolution, belong to space group P3121 (or P3221) with a = 48.86, c = 78.61 Å, and contain one molecule per asymmetric unit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996005513
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  • 10
    Electronic Resource
    Electronic Resource
    Phase extension and refinement of Bence–Jones protein Rhe (1.9 Å) (1979)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 35 (1979), S. 810-817 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A procedure is described whereby crude atomic coordinates obtained from a medium-resolution electron density map (3̃-4 Å) with the aid of Watson-Kendrew models may be refined to native data of near-atomic resolution using only a limited subset of the data and non-interactive computer graphics. This refinement procedure for the Bence-Jones protein Rhe included phase extension from 3.0 to 1.9 Å and led to an improved crystallographic sequence for the protein. The structure was refined, by a stereochemically restrained least-squares technique in reciprocal space, to a residual value RF = 0.284 for a model consisting of 795 non-hydrogen protein atoms with an overall thermal factor using data with d ranging from 5.0 to 1.9 Å. Relative weights for the structure factor and stereochemical-restraint observations were determined empirically and the optimum weights were found to be those which yield values of W|Fo - Fc|2 which are typically 4 to 6 times the value of W|do - dI|2, where do and dI are the current and ideal values for the stereochemically restrained parameters. It was found that reasonable refinement may be obtained with only 32% of the observed data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739479001832
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