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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization of engineered Thermus flavus 5S rRNA under earth and microgravity conditions (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 498-500 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Thermus flavus 5S rRNA with a molecular weight of about 40 kDa was modified at the 5′ and 3′ ends. Crystals were obtained under earth and microgravity conditions. The best crystals were obtained during NASA space mission STS 94. For the first time, it was possible to collect a complete data set from 5S rRNA crystals to 7.8 Å resolution and to assign the space group as R32, with unit-cell parameters a = b = 110.3, c = 387.6 Å, α = β = 90, γ = 120°.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900001736
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 999-1001 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystallization of the hydrophilic ectodomain of the epidermal growth factor (EGF) receptor has been accomplished in the presence of the ligand EGF. Two different crystal forms have been obtained, one of which was suitable for X-ray analysis. The space group of this form has been assigned to P21212 with unit-cell dimensions of a = 207.4, b = 113.3 and c = 120.4 Å. A native data set has been recorded and a heavy-atom search is currently under way. Diffraction from these crystals, however, is limited to low resolution and extensive trials to improve crystal quality further have all failed. To analyse the molecular shape and aggregation of the receptor protein in solution, small-angle X-ray diffraction and dynamic light-scattering techniques have been applied. Synchrotron radiation in combination with cryo-techniques is essential for data collection because of the high solvent content and radiation sensitivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998001851
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of the neurotoxic, heterodimeric phospholipase A2 from the Taiwan viper (Vipera russelli formosensis) (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1064-1065 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The 28 kDa heterodimeric complex from Taiwan viper (F4/F7 complex) is composed of a neurotoxic phospholipase A2 (F4) and a non-toxic PLA2-like component (F7). Despite a high sequence identity (65%), the biological and pharmacological activities of F4 and F7 are contrasting. The complex is a structural analogue of Vipoxin found in the venom of the Bulgarian viper Vipera ammodites meridionalis. It is unclear how and why such varied bioactivities are expressed in these similar components. The F4/F7 complex has been crystallized using hanging-drop vapour diffusion and macroseeding techniques. The space group is monoclinic P2_1 with unit-cell dimensions a=74.92, b=85.13, c=78.16 Å and \beta=95.12°. X-ray intensity data to 2.0 Å resolution have been collected at 120 K and the structure has been solved using the molecular-replacement method. There are four F4/F7 complex molecules in the asymmetric unit, which do not exhibit any local point-group symmetry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999002735
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  • 4
    Electronic Resource
    Electronic Resource
    Atomic structure of the Serratia marcescens endonuclease at 1.1 Å resolution and the enzyme reaction mechanism (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 567-572 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional crystal structure of Serratia marcescens endonuclease has been refined at 1.1 Å resolution to an R factor of 12.9% and an Rfree of 15.6% with the use of anisotropic temperature factors. The model contains 3694 non-H atoms, 715 water molecules, four sulfate ions and two Mg2+-binding sites at the active sites of the homodimeric protein. It is shown that the magnesium ion linked to the active-site Asn119 of each monomer is surrounded by five water molecules and shows an octahedral coordination geometry. The temperature factors for the bound Mg2+ ions in the A and B subunits are 7.08 and 4.60 Å2, respectively, and the average temperature factors for the surrounding water molecules are 12.13 and 10.3 Å2, respectively. In comparison with earlier structures, alternative side-chain conformations are defined for 51 residues of the dimer, including the essential active-site residue Arg57. A plausible mechanism of enzyme function is proposed based on the high-resolution S. marcescens nuclease structure, the functional characteristics of the natural and mutational forms of the enzyme and consideration of its structural analogy with homing endonuclease I-PpoI.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744490000322X
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  • 5
    Electronic Resource
    Electronic Resource
    Preliminary X-ray diffraction studies of the external functional unit RtH2-e from the Rapana thomasiana (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1663-1665 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The `external' oxygenated functional unit RtH2-e of the Rapana hemocyanin subunit RHSS2 was isolated and crystallized. X-ray intensity data to 3.3 Å resolution have been collected at 100 K and the structure has been solved using the molecular-replacement method. The space group is assigned to be the tetragonal P43212, with unit-cell parameters a = b = 105.5, c = 375.0 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012124
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  • 6
    Electronic Resource
    Electronic Resource
    Regulation of catalytic function by molecular association: structure of phospholipase A2from Daboia russelli pulchella (DPLA2) at 1.9 Å resolution (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1793-1798 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of phospholipase A2 from the venom of Daboia russelli pulchella has been refined to an R factor of 0.216 using 17 922 reflections to 1.9 Å resolution. The structure contains two crystallographically independent molecules in the asymmetric unit. The overall conformations of the two molecules are essentially the same except for three regions, namely the calcium-binding loop including Trp31, the β-wing and the C-terminal residues 119–131. Although these differences have apparently been caused by molecular packing, they seem to have functional relevance. Particularly noteworthy is the conformation of Trp31, which is favourable for substrate binding in one molecule as it is aligned with one of the side walls of the hydrophobic channel, whereas in the other molecule it is located at the mouth of the channel, thereby blocking the entry of substrates leading to loss of activity. This feature is unique to the present structure and does not occur in the dimers and trimers of other PLA2s.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901014524
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  • 7
    Electronic Resource
    Electronic Resource
    Structure of the bifunctional inhibitor of trypsin and α-amylase from ragi seeds at 2.2 Å resolution (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 287-293 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of a bifunctional inhibitor of α-amylase and trypsin (RATI) from ragi seeds (Indian finger millet, Eleusine coracana Gaertneri) has been determined by X-ray diffraction at 2.2 Å resolution. The inhibitor consists of 122 amino acids, with five disulfide bridges, and belongs to the plant α-amylase/trypsin inhibitor family. The crystals were grown by the microdialysis method using ammonium sulfate as a precipitating agent. The structure was determined by the molecular-replacement method using as models the structures of Corn Hageman factor inhibitor (CHFI) and of RATI at 2.9 Å resolution determined previously. It has been refined to an R factor of 21.9%. The structure shows an r.m.s. deviation for Cα atoms of 2.0 Å compared with its own NMR structure, whereas the corresponding value compared with CHFI is found to be 1.4 Å. The r.m.s. difference for Cα atoms when compared with the same protein in the structure of the complex with α-amylase is 0.7 Å. The conformations of trypsin-binding loop and the α-amylase-binding N-terminal region were also found to be similar in the crystal structures of native RATI and its complex with α-amylase. These regions differed considerably in the NMR structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999016601
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  • 8
    Electronic Resource
    Electronic Resource
    Structure of an RNA duplex with an unusual G·C pair in wobble-like conformation at 1.6 Å resolution (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 219-224 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of the RNA duplex r(CUGGGCGG)·r(CCGCCUGG) has been determined at 1.6 Å resolution and refined to a final R factor of 18.3% (Rfree = 24.1%). The sequence of the RNA fragment resembles domain E of Thermus flavus 5S rRNA. A previously undescribed wobble-like G·C base-pair formation is found. Owing to the observed hydrogen-bond network, it is proposed that the cytosine is protonated at position N3. The unusual base-pair formation is presumably strained by intermolecular interactions. In this context, crystal packing and particular intermolecular contacts may have direct influence on the three-dimensional structure. Furthermore, this structure includes two G·U wobble base pairs in tandem conformation, with the purines forming a so-called `cross-strand G stack'.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900017042
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation, purification, crystallization and preliminary X-ray analysis of β1-bungarotoxin from Bungarus caeruleus (Indian common krait) (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1093-1094 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: β-Bungarotoxin is a heterodimeric neurotoxin consisting of a phospholipase A2 subunit linked by a disulfide bond to a K+ channel binding subunit, which is a member of of the Kunitz protease-inhibitor subfamily. Purified β1-bungarotoxin was crystallized using microdialysis techniques. The rectangular-shaped crystals are orthorhombic, space group C2221, with unit-cell dimensions a = 80.7, b = 82.5, c = 56.9 Å. The crystals have a calculated Vm of 2.35 Å3 Da−1 for one molecule in the asymmetric unit. This corresponds to a solvent content of 48%. X-ray intensity data were collected to 2.6 Å resolution. The data set is 97.4% complete.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999003285
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  • 10
    Electronic Resource
    Electronic Resource
    Cyclohexylammonium μ-disulfido-bis(trioxophosphate)(4–) monohydrate, 4C6H14N4+.O6P2S24−.H2O (1983)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 39 (1983), S. 270-273 
    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/S0108270183004369
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