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  • 1
    Electronic Resource
    Electronic Resource
    Structure of cytochrome c2 from Rhodospirillum centenum (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1498-1505 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Cytochrome c2 from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 Å, and diffract to a resolution limit of 1.7 Å. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended α-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901010423
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  • 2
    Electronic Resource
    Electronic Resource
    Amphiphiles modify the properties of detergent solutions used in crystallization of membrane proteins (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 925-927 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The effect of the amphiphile heptanetriol on the properties of solutions containing several detergents commonly used for crystallization of membrane proteins was characterized. The critical micelle concentration was found to be relatively unchanged by the presence of the amphiphile. In contrast, the addition of heptanetriol to solutions containing both detergent and polyethylene glycol exhibited significant shifts in the clouding behavior, with the largest shifts being for lauryl dimethylamine oxide. These results suggest that conditions favorable for crystallization of integral membrane proteins can be inferred from the properties of the detergents and amphiphiles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744490100378X
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  • 3
    Electronic Resource
    Electronic Resource
    Individual interactions influence the crystalline order for membrane proteins (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1281-1286 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The role of contact interactions in the crystallization of membrane proteins was assessed by mutation of amino-acid residues on the surface of the reaction center from Rhodobacter sphaeroides. Five single-site mutants were constructed, with changes in contact regions found in the trigonal and tetragonal forms but not the orthorhombic form. Crystallization trials for the tetragonal form yielded either no crystals or crystals with an altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the tetragonal crystals. Changes in the structures determined by X-ray diffraction of trigonal crystals for each mutant were related to the quality of the diffraction. Significant differences in the resolution limit of the crystals were associated with the loss of specific interactions between neighboring proteins. The results suggest that the contact regions are crucial for obtaining highly ordered crystals of membrane proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744490101109X
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and X-ray structure determination of cytochrome c2 from Rhodobacter sphaeroides in three crystal forms (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 596-602 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Cytochrome c2 serves as the secondary electron donor that reduces the photo-oxidized bacteriochlorophyll dimer in photosynthetic bacteria. Cytochrome c2 from Rhodobacter sphaeroides has been crystallized in three different forms. At high ionic strength, crystals of a hexagonal space group (P6122) were obtained, while at low ionic strength, triclinic (P1) and tetragonal (P41212) crystals were formed. The three-dimensional structures of the cytochrome in all three crystal forms have been determined by X-ray diffraction at resolutions of 2.20 Å (hexagonal), 1.95 Å, (triclinic) and 1.53 Å (tetragonal). The most significant difference observed was the binding of an imidazole molecule to the iron atom of the heme group in the hexagonal structure. This binding displaces the sulfur atom of Met l00, which forms the axial ligand in the triclinic and tetragonal structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994001319
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of the 51 kDa protein of the mosquito-larvicidal binary toxin from Bacillus sphaericus (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1083-1085 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Certain strains of Bacillus sphaericus produce a highly toxic mosquito-larvicidal protein during sporulation which is active against vectors of dengue, encephalitis and malaria. This toxin is initially expressed as 51 and 42 kDa proteins and is converted to 43 and 39 kDa proteins, respectively, which form the active heterodimer complex. For a better understanding of the toxicity mechanism at the molecular level, the 51 kDa protein of the binary toxin of B. sphaericus strain 2297 was expressed as a glutathione-S-transferase fusion protein and purified by affinity chromatography. Protein crystals were grown from an amorphous precipitate in five months using the hanging-drop vapor-diffusion method. The protein crystals were dissolved and were found to be composed of a proteolytically modified 45.2 kDa derivative similar to the active form of this protein. The crystals form in space group P43212 (or P41212) and diffract to 2.6 Å, with unit-cell dimensions a = b = 133.48, c = 69.76 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999003157
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  • 6
    Electronic Resource
    Electronic Resource
    Organophosphorus Insecticides. 16. Azinphos Ethyl: O,O-Diethyl S-{[4-Oxo-1,2,3-benzotriazin-3(4H)-yl]methyl} Phosphorodithioate, C12H16N3O3PS2 (1995)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 521-523 
    Details
    ISSN: 1600-5759
    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/S0108270194007705
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