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  • 1
    Electronic Resource
    Electronic Resource
    Structure of the Brain-Derived Neurotrophic Factor/Neurotrophin 3 Heterodimer (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 4139-4146 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00013a001
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  • 2
    Electronic Resource
    Electronic Resource
    Recognition surfaces of MHC class I (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 163 (1998), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: Recent crystallographic results have provided dose to atomic resolution views of the recognition events mediated by MHC class I molecules. The specificity-conferring interaction of MHC class I/peptide with a T-cell antigen receptor (TCR) appears dependent on certain key interactions with the MHC scaffold. These interactions, in particular those of the TCR Va domain, define a standard orientation for TCR binding. Previous studies on biologically significant variations in the TCR recognition surface presented by a series of MHC/variant peptide complexes can be reassessed in the light of this TCR-building mode. The interaction of CDS with MHC class I resembles that between antibody and antigen in the use of loops from the CD8 structure. The interaction is of very low affinity and buries equivalent surface area to that between the TCR and MHC class I but while the TCR/MHC interface shows poor surface shape complementarity the match in the conservative interaction between MHC and CDS is precise.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-065X.1998.tb01191.x
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  • 3
    Electronic Resource
    Electronic Resource
    Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution (1978)
    [s.l.] : Nature Publishing Group
    Nature 271 (1978), S. 626-630 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The structure determination of pyruvate kinase shows that each subunit of the tetrameric molecule consists of three domains. The largest of these domains has a remarkable similarity to the structure of triosephosphate isomerase. Another domain shows similarities to many other nucleotide binding ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/271626a0
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  • 4
    Electronic Resource
    Electronic Resource
    Building meaningful models of glycoproteins (2007)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 14 (2007), S. 354-354 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To the Editor: The building of crystallographic models of proteins is guided by understanding of the primary structure of proteins and by well-established and rigorously applied stereochemical principles. However, a cursory survey of Protein Data Bank entries containing oligosaccharides suggests ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb0507-354a
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  • 5
    Electronic Resource
    Electronic Resource
    Bluetongue virus VP4 is an RNA-capping assembly line (2007)
    [s.l.] : Nature Publishing Group
    Nature structural & molecular biology 14 (2007), S. 449-451 
    Details
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Eukaryotic organisms cap the 5′ ends of their messenger RNAs by a series of four chemical reactions. Some viruses achieve this using a single molecule; the crystal structure of such an enzyme from bluetongue virus reveals an elongated modular architecture that provides a scaffold for an ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsmb1225
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray crystallographic studies on the bacteriophage Φ6 RNA-dependent RNA polymerase (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1473-1475 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The RNA-dependent RNA polymerase (P2) from bacteriophage Φ6 has been cloned and the protein overexpressed in Escherichia coli to produce an active enzyme. A fully substituted selenomethionyl version of the protein has also been produced. Crystals of both proteins have been grown; most belong to the monoclinic space group P21, with unit-cell parameters a = 105.9, b = 94.0, c = 140.9 Å, β = 101.4°, but some are trigonal (space group P31 or P32), with unit-cell parameters a = b = 110.1, c = 159.4 Å, γ = 120°. Both crystal forms occur in the same crystallization drop and are morphologically indistinguishable. Native data sets have been collected from both types of crystals to better than 3 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900010702
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and functional analysis of a soluble deglycosylated form of the human costimulatory molecule B7-1 (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 605-608 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The interactions of B7-1 with CD28 and CTLA-4 modulate the course of human immune responses, making B7-1 an important target for developing structure-based therapeutics. B7-1 is, however, one of the most heavily glycosylated proteins found at the leukocyte cell surface, complicating the structural analysis of this molecule. Methods for the production, crystallization and selenomethionine labelling of a soluble deglycosylated form of this molecule are described. The protein readily forms both tetragonal plate and bipyramidal crystals belonging to space groups I4122, with unit-cell parameters a = b = 56.9, c = 298.7 Å, and P4122 (or P4322), with unit-cell parameters a = b = 89.0, c = 261.9 Å, respectively. The I4122 and primitive crystal forms diffract to 2.7 and 3.5 Å, respectively. Surface plasmon resonance-based assays indicate that the ligand-binding properties of sB7-1 are unaffected by deglycosylation. Since none of the methods relied on any special structural properties of sB7-1, it is proposed that this novel combination of procedures could in principle be adapted to the systematic analysis of many other glycoproteins of structural or functional interest.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901001895
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  • 8
    Electronic Resource
    Electronic Resource
    Continuous and Discontinuous Changes in the Unit Cell of HIV-1 Reverse Transcriptase Crystals on Dehydration (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 938-953 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A crystal form of HIV-1 reverse transcriptase (RT) complexed with inhibitors showed diffraction to a high-resolution limit of 3.7 Å. Instability in the unit-cell dimensions of these crystals was observed during soaking experiments, but the range of this variability and consequent change in lattice order was revealed by a chance observation of dehydration. Deliberately induced dehydration results in crystals having a variety of unit cells, the best-ordered of which show diffraction to a minimum Bragg spacing of 2.2 Å. In order to understand the molecular basis for this phenomenon, the initial observation of dehydration, the data sets from dehydrated crystals, the crystal packing and the domain conformation of RT are analysed in detail here. This analysis reveals that the crystals undergo remarkable changes following a variety of possible dehydration pathways: some changes occur gradually whilst others are abrupt and require significant domain rearrangements. Comparison of domain arrangements in different crystal forms gives insight into the flexibility of RT which, in turn, may reflect the internal motions allowing this therapeutically important enzyme to fulfill its biological function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998004284
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  • 9
    Electronic Resource
    Electronic Resource
    Complementing crystallography: the role of cryo-electron microscopy in structural biology (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1742-1749 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Dramatic improvements in experimental methods and computational techniques have revolutionized three-dimensional image reconstruction from electron micrographs (EM) of vitrified samples. Recent results include the first determination of a protein fold (for the core protein of the hepatitis B virus) by non-crystalline imaging techniques. These developments have generated interest within the crystallographic community and have led to a re-evaluation of the technique, particularly amongst those working in the field of virus structure or struggling with the phasing of large macromolecular assemblies. A simple discussion of the techniques of EM image reconstruction and its advantages and problems in terms familiar to crystallographers will hopefully allow an appreciation of the essential complementarity of the two techniques and the practical potentials for phasing applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999009956
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  • 10
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary diffraction studies of the extracellular region of human p58 killer cell inhibitory receptor (KIR2) (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 433-435 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Molecules of the human killer cell inhibitory receptor (KIR) family, which belong to the immunoglobulin superfamily (IgSF), are expressed on the surface of natural killer (NK) cells and some subsets of T cells. These receptors function to mediate the inhibition or activation of cytotoxic activity by recognizing HLA class I molecules on the target cell. The extracellular region of a p58 KIR specific for HLA-Cw1,3,7 (KIR2) has been overproduced in Escherichia coli and purified. The recombinant KIR2 has been crystallized in 9–10% poly(ethylene glycol) methyl ether (average Mr = 8000), 50mM HEPES, 8% ethylene glycol, 0.5% octyl-β-glucoside, pH 7.5, at 294 K using the sitting-drop vapour-diffusion method. Preliminary X-ray diffraction studies reveal the space group to be hexagonal (P6122 or P6522) with lattice constants a = b = 95.3, c = 130.8 Å. A native data set (3 Å resolution) has been collected at the Photon Factory (λ = 1.0 Å).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997012201
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