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  • 11
    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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  • 12
    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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  • 13
    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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  • 14
    Electronic Resource
    Electronic Resource
    The use of phase combination in the refinement of phosphoglycerate kinase at 2.5 Å resolution (1981)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 37 (1981), S. 491-500 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The combination of phase information obtained by the method of isomorphous replacement with that calculated from a partial model of the structure has proved to be a powerful tool in the interpretation of the structure of horse muscle phosphoglycerate kinase. That the combined phases are an improvement on the calculated or isomorphous ones is evidenced by more readily interpretable electron density maps, which show only a low level of feedback from incorrectly located atoms. Several different types of Fourier syntheses have been calculated using the combined phase angles and an essentially qualitative evaluation of their relative merits is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739481001186
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  • 15
    Electronic Resource
    Electronic Resource
    Crystallization of the glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1185-1187 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NADP+-dependent glutamate dehydrogenase from Thermococcus litoralis has been crystallized by the hanging-drop method of vapour diffusion using an ammonium sulfate and PEG mixture as the precipitant. The crystals belong to the monoclinic system and are in space group C2 with unit-cell dimensions a = 142.7, b = 202.0, c = 125.8 Å with β = 113.1° with a hexamer in the asymmetric unit. T. Litoralis, a hyperthermophilic organism, belongs to the family of Archaea and has a maximum growth temperature of about 370 K. The glutamate dehydrogenase isolated from this organism has a half-life of 2 h at 373 K and a comparison of this structure with that of other GluDH's from hyperthermophilic organisms and from mesophiles will contribute to an understanding of the molecular mechanisms which underlie thermostability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996007421
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  • 16
    Electronic Resource
    Electronic Resource
    Crystallization of cytochrome b562 from Erwinia chrysanthemi (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 197-199 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Cytochrome b562 from Erwinia chrysanthemi has been crystallized using the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. X-ray precession photographs show that the crystals formed belong to either of the enantiomorphic space groups P41212 or P43212 with the cell parameters a = b = 98.6 and c = 62.7 Å. Estimation of the crystal density and consideration of the possible values for Vm indicate that there is either a dimer or trimer in the asymmetric unit. Experiments using the synchrotron radiation source at the CCLRC Daresbury Laboratory have shown that the crystals diffract to at least 2.7 Å resolution. An analysis of the N-terminal sequence indicates that this cytochrome shows limited homology to the cytochrome b562 from E. coli. Determination of the structure will therefore allow analysis of the relationship between these two proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996011201
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  • 17
    Electronic Resource
    Electronic Resource
    Crystallization of the alanine dehydrogenase from Phormidium lapideum (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 407-408 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Amino-acid dehydrogenases catalyse the interconversion of their respective amino acids to the corresponding keto acid, with concomitant reduction of NAD or NADP. The enzymes phenylalanine, glutamate, leucine and valine dehydrogenase all share a similar three-dimensional subunit structure and a high degree of sequence similarity, indicating that they belong to an enzyme superfamily related by divergent evolution. In contrast, alanine dehydrogenase shows no sequence similarity with any of these enzymes despite catalysing a reaction with the same chemistry and thus it is predicted that it possesses a different three-dimensional structure. The alanine dehydrogenase from Phormidium lapideum has been crystallized in space group R32, cell dimensions a = b = 123.1 and c = 184.8 Å, with a monomer in the asymmetric unit. The structure determination of this enzyme will shed light on how nature has evolved two different systems to carry out the same reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997011578
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  • 18
    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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  • 19
    Electronic Resource
    Electronic Resource
    Crystallization of Escherichia coli enoyl reductase and its complex with diazaborine (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1181-1184 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Recent work has shown that the NADH-dependent enoyl acyl carrier protein reductase from Escherichia coli is the target for diazaborine, an antibacterial agent. This enzyme has been crystallized by the hanging-drop method of vapour diffusion complexed with NAD+ and in the presence and absence of a thieno diazaborine. The crystals grown in the absence of diazaborine (form A) are in the space group P21 with unit-cell dimensions a = 74.0, b = 81.2, c = 79.0 Å and β = 92.9°, and with a tetramer in the asymmetric unit, whilst those grown in the presence of diazaborine (form B) are in the space group P6122 (or P6522) with unit-cell dimensions a = b = 80.9 and c = 328.3 Å, and with a dimer in the asymmetric unit. The structure determination of this enzyme in the presence of diazaborine will provide information on the nature of the drug binding site and contribute to a programme of rational drug design.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996005458
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  • 20
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata) (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 451-453 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P212121, with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 Å, α = β = γ = 90° and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 Å resolution have been collected in-house using a MAR 345 imaging-plate system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901000257
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