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  • 1
    Electronic Resource
    Electronic Resource
    The structures of the monoclinic and orthorhombic forms of hen egg-white lysozyme at 6 Å resolution (1982)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 38 (1982), S. 778-783 
    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/S0567740882004075
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  • 2
    Electronic Resource
    Electronic Resource
    Dramatic increase in ferritin crystal lifetime with monochromatic synchrotron X-radiation tuned to a wavelength above the iron K absorption edge (1989)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 22 (1989), S. 284-286 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A dramatic increase in the lifetime of ferritin crystals during single-crystal X-ray diffraction data collection has been observed in experiments with monochromatic synchrotron X-radiation tuned to a wavelength slightly above the iron K absorption edge.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889889000518
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme (1979)
    [s.l.] : Nature Publishing Group
    Nature 279 (1979), S. 773-777 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase has yielded the complete sequence and structure of the horse muscle enzyme. Metal ADP and ATP substrates are bound to one of the two widely separated domains in an environment that seems unsuitable for ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/279773a0
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  • 4
    Electronic Resource
    Electronic Resource
    Isomorphous replacement with optimized anomalous scattering applied to protein crystallography (1990)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 46 (1990), S. 721-725 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Isomorphous replacement is an essential technique for the de novo solution of macromolecular crystal structures. The use of the anomalous-dispersion effect of the heavy atom in the derivative leads to the acronyms SIRAS or MIRAS (single or multiple isomorphous replacement with anomalous scattering) as the term for the phase determination method. Synchrotron radiation is tuneable over a wavelength range encompassing the absorption edges of the typically used derivative atoms such as Hg, Au and Pt. Hence, it is possible to optimize the anomalous-scattering signal of such atoms by appropriate choice of a wavelength between 0̃.8 and 1.1 Å. This paper reports a comparison of this method (which we call SIROAS; O for optimized) and SIRAS on related mercury derivatives of glutamate dehydrogenase. The anomalous-scattering signal is enhanced in the SIROAS experiment and this results in an increase of the phasing power of the derivative data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108767390005153
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization of glycerol dehydrogenase from Bacillus stearothermophilus (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 830-832 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NAD+-linked glycerol dehydrogenase from Bacillus stearothermophilus is a member of the so-called `iron- containing' class of polyol dehydrogenases. This enzyme has been crystallized in three different forms in the presence of a range of divalent cations and glycerol or NAD+ using the hanging-drop method of vapour diffusion with ammonium sulfate as the precipitant. X-ray photographs have established that the crystals grown in the presence of zinc and glycerol (form A) most likely belong to space group I4122 with cell parameters a = b = 102 and c = 728 Å. The crystals grown with zlnc and NAD+ (form B) belong to the tetragonal system and probably belong to the space group P4212 with cell parameters a = b = 150 and c = 220 Å. The crystals grown with lead and glycerol (form C) belong to a primitive orthorhombic system with cell parameters a = 127, b = 178 and c = 173 Å. Experiments using the synchrotron radiation source at the DRAL Daresbury laboratory have shown all three crystal types diffract to at least 3 Å resolution. Elucidation of the three-dimensional structure of this enzyme will provide a structural framework for this class of polyol dehydrogenases, which are not represented in the database at present, and enable comparisons to be made with enzymes belonging to the other classes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994013533
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization of NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239 (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 269-272 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NAD+-dependent phenylalanine dehydrogenase from Nocardia sp239 has been crystallized by the hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Two crystal forms were obtained in the presence and absence of the enzyme substrates phenylpyruvic acid or phenylalanine and its coenzyme NADH. Crystals of the native protein belong to the hexagonal system, with the space group being one of the enantiomorphic pair P6122 or P6522. The cell dimensions are a = b = 111.0, c = 174.5 Å, α = β = 90 and γ = 120°. Crystals grown from the protein co-crystallized with its substrates all belong to the trigonal system, space group P3121 or P3221, with unit-cell dimensions of a = b = 88.1 , c = 112.6 Å, α = β = 90 and γ = 120°. Preliminary protein-sequencing experiments have established that this enzyme is related to the octameric PheDH's which are members of the wider superfamily of amino-acid dehydrogenases. However, gel-filtration studies suggest that this enzyme is active as a monomer. The full determination of the three-dimensional structure of this phenylalanine dehydrogenase will add to the understanding of the molecular basis of the differential substrate specificity within this enzyme superfamily. In turn this will contribute to the rational design of an amino-acid dehydrogenase which could be used for the diagnosis of phenylketonuria and for the chiral synthesis of high-value pharmaceuticals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997009980
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of Citrobacter amalonaticus methylaspartate ammonia lyase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1922-1924 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Methylaspartate ammonia lyase (MAL) catalyses the reversible α,β-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to give mesaconic acid. Crystals of Citrobacter amalonaticus MAL have been obtained by the hanging-drop method of vapour diffusion using ammonium sulfate as the precipitant. Three crystal forms were obtained from identical crystallization conditions, two of which (forms A and B) diffract to high resolution, whilst the third form diffracted poorly. Crystals of form A diffract to beyond 2.1 Å and have been characterized as belonging to one of the enantiomorphic space groups P4122 or P4322, with unit-cell parameters a = b = 66.0, c = 233.1 Å, α = β = γ = 90° and a monomer in the asymmetric unit. Crystals of form B diffract to beyond 1.5 Å and belong to space group C222, with unit-cell parameters a = 128.3, b = 237.4, c = 65.8 Å, α = β = γ = 90° and a dimer in the asymmetric unit. Determination of the structure of MAL will be an important step in resolving current conflicts concerning the enzyme mechanism which differ between one which places MAL as a member of the superfamily of ammonia lyases whose catalytic activity requires a cofactor formed by post-translational modification of the enzyme and another which links MAL to the enolase superfamily.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901016675
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  • 8
    Electronic Resource
    Electronic Resource
    Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 240-242 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NAD(P)-dependent glutamate dehydrogenase from Pyrococcus furiosus has been crystallized by the hanging-drop method of vapour diffusion using lithium sulfate as the precipitant. The crystals belong to the tetragonal system and are in space group P42212 with unit-cell dimensions of a = b = 167.2, c = 172.9 Å. Consideration of the values of Vm and possible packing of the molecules within the cell suggest that the asymmetric unit contains a trimer. P. furiosus belongs to the family of Archaea and is one of the most thermostable organisms known, having an optimal growth temperature of 376 K. The glutamate dehydrogenase isolated from this organism has a half-life of 12 h at 373 K and, therefore, the determination of the structure of this enzyme will be important in advancing our understanding of how proteins are adapted to enable them to survive at such extreme temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994012862
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  • 9
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the NADP-specific glutamate dehydrogenase from Neurospora crassa (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 837-839 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NADP-linked glutamate dehydrogenase from Neurospora crassa has been crystallized by the hanging-drop method of vapour diffusion in the presence of 0.1 M glutamate. The crystals are trigonal and are in space group P3121 with unit-cell dimensions of a = b = 196.6, c = 102.0 Å and with a trimer in the asymmetric unit. A full structure determination of this enzyme will lead to an understanding of the molecular basis of inter-allelic complementation observed with hybrid hexamers of naturally occurring mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995000904
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  • 10
    Electronic Resource
    Electronic Resource
    Crystallization and analysis of the subunit assembly and quaternary structure of imidazoleglycerol phosphate dehydratase from Saccharomyces cerevisiae (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 845-847 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Imidazoleglycerol phosphate dehydratase (IGPD) from Saccharomyces cerevisiae has been crystallized in the presence of a range of divalent cations using the hanging-drop method of vapour diffusion with ammonium sulfate or polyethylene glycol (PEG) 4000 as the precipitants. X-ray precession photographs have established that the crystals formed with ammonium sulfate (form A) belong to the space group F432, with cell parameter a = 177.5 Å and a single subunit in the asymmetric unit. A preliminary data set collected to 6 Å resolution on a two-detector San Diego Multiwire area detector has established that the crystals formed with PEG 4000 (form B) belong to either of the special pair of space groups I23 or I213, with cell parameter a = 131.0 Å. A self-rotation function has been calculated using these data and indicates that the cell axes show pseudo fourfold symmetry consistent with a dimer in the asymmetric unit in this crystal form. Light-scattering studies indicate that in the presence of Mn2+ and a number of other divalent cations IGPD undergoes assembly to a particle of molecular weight approximately 500 kDa. Given the subunit molecular weight of 23 kDa together with the symmetry of the crystals it would indicate that the most likely quaternary structure for this enzyme is based on a 24-mer in 432 symmetry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995001569
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