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  • Springer Nature  (19)
  • Springer  (15)
  • International Union of Crystallography (IUCr)  (14)
  • 2000-2004  (48)
  • 1965-1969
  • 1955-1959
  • 2001  (48)
  • 1
    Electronic Resource
    Electronic Resource
    Subunit dissociation and reassociation leads to preferential crystallization of haemoglobin Bart's (γ4) from solutions of human embryonic haemoglobin Portland (ζ2γ2) at low pH (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 921-924 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A variety of human haemoglobins (Hbs) are produced at different stages of human development, including three embryonic Hbs, foetal Hb and adult Hb. All are heterotetramers. During crystallization experiments on human embryonic Hb Portland (ζ2γ2), it was discovered by crystallographic and biochemical analysis that the homotetramer Hb Bart's (γ4) preferentially crystallizes from ζ2γ2 solutions below pH 5. This results from dissociation of Hb Portland into γ2 dimers and ζ monomers and has interesting implications for subunit interactions and tetramer stability in Hbs. It also makes possible a full crystallographic analysis of Hb Bart's, which is of considerable medical significance because of its presence in the red blood cells of millions of people worldwide who suffer from α-thalassaemia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901004516
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  • 2
    Electronic Resource
    Electronic Resource
    Expression, crystallization and preliminary characterization of methylmalonyl coenzyme A epimerase from Propionibacterium shermanii (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 706-708 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Methylmalonyl-CoA epimerase (MMCE) is an enzyme that interconverts the R and S epimers of methylmalonyl-CoA in the pathway that links propionyl-CoA with succinyl-CoA. This is used for both biosynthetic and degradative processes, including the breakdown of odd-numbered fatty acids and some amino acids. The enzyme has been expressed in Escherichia coli both as the native enzyme and as its selenomethionine (SeMet) derivative. Crystals of both forms have been obtained by vapour diffusion using monomethylether PEG 2000 as precipitant. The native MMCE crystals are orthorhombic, with unit-cell parameters a = 56.0, b = 114.0, c = 156.0 Å, and the SeMet-MMCE crystals are monoclinic, with unit-cell parameters a = 43.6, b = 78.6, c = 89.4 Å, β = 92.0°; both diffract to better than 2.8 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901002050
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  • 3
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    Mae mediates MAP kinase phosphorylation of Ets transcription factors in Drosophila (2001)
    Springer Nature
    Details
    Publication Date: 2001-05-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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    PAPER CURRENT
  • 4
    Electronic Resource
    Electronic Resource
    Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 480-487 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of a tryptophan-containing variant of the IgG-binding B1 domain of protein L has been solved in two crystal forms to 1.7 and 1.8 Å resolution. In one of the crystal forms, the entire N-terminal histidine-tag region was immobilized through the coordination of zinc ions and its structural conformation along with the zinc coordination scheme were determined. However, the ordering of the histidine tag by zinc does not affect the overall structure of the rest of the protein. Structural comparisons of the tryptophan-containing variant with an NMR-derived wild-type structure, which contains a tyrosine at position 47, reveals a common fold, although the overall backbone root-mean-square difference is 1.5 Å. The Y47W substitution only caused local rearrangement of several side chains, the most prominent of which is the rotation of the Tyr34 side chain, resulting in a 6 Å displacement of its hydroxyl group. A small methyl-sized cavity bounded by β-strands 1, 2 and 4 and the α-helix was found in the structures of the Y47W-substituted protein L B1 domain. This cavity may be created as the result of subsequent side-chain rearrangements caused by the Y47W substitution. These high-resolution structures of the tryptophan-containing variant provide a reference frame for the analysis of thermodynamic and kinetic data derived from a series of mutational studies of the protein L B1 domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901000373
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  • 5
    Electronic Resource
    Electronic Resource
    Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 759-762 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Structural studies of the wild type and mutants of the src SH3 domain were initiated to elucidate the correlation of the native-state topology with protein thermostability and folding kinetics. An extra mass of 178 Da arising from the post-translational modification at the N-terminal His tag was observed. The spontaneous α-N-6 gluconoylation at the amino group of the His-tagged SH3 domain contributed to the observed extra mass. The partial modification of the N-terminal His-tag produced heterogeneity, both in size and in charge, in the Escherichia coli expressed SH3 domain. The removal of the His tag from the SH3 domain was essential for the crystallization of both wild-type and mutant src SH3. Both the wild type and the W43I mutant were crystallized by hanging-drop vapor diffusion and are in the hexagonal space group P6522 with one molecule in the asymmetric unit. Data sets were collected to 1.8 and 1.95 Å resolution for the the wild type and the W43I mutant, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901002918
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Haloferax mediterranei (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1887-1889 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Glucose dehydrogenase (E.C 1.1.1.47; GlcDH) from Haloferax mediterranei has been overexpressed in Escherichia coli, solubilized by the addition of 8 M urea and refolded by rapid dilution. The protein has been purified by conventional techniques and crystallized by the hanging-drop vapour-diffusion method using sodium citrate as the precipitant. Two crystal forms representing the free enzyme and the binary complex with NADP+ grow under these conditions. Crystals of form I diffract to beyond 3.5 Å resolution and belong to the hexagonal space group P622, with unit-cell parameters a = b = 89.1, c = 214.6 Å, α = β = 90, γ = 120°. Crystals of form II diffract to greater than 2.0 Å and belong to the orthorhombic space group I222 or I212121, with unit-cell parameters a = 61.8, b = 110.9, c = 151.7 Å, α = β = γ = 90°. Calculated values for VM and consideration of the packing for both crystal forms suggests that the asymmetric units in both crystal forms contain a monomer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901015189
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  • 7
    Electronic Resource
    Electronic Resource
    Purification, crystallization and quaternary structure analysis of a glycerol dehydrogenase S305C mutant from Bacillus stearothermophilus (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 165-167 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) is a 39.5 kDa molecular weight metalloenzyme which catalyzes the oxidation of glycerol to dihydroxyacetone with the concomitant reduction of NAD+ to NADH. Despite its classification as a member of the `iron-containing' polyol dehydrogenase family, studies on recombinant B. stearothermophilus GlyDH have shown this enzyme to be Zn2+-dependent. Crystals of a S305C GlyDH mutant were obtained by the hanging-drop vapour-diffusion method, using ammonium sulfate and PEG 400 as precipitating agents, in the presence and absence of NAD+. The crystals belong to space group I422, with approximate unit-cell parameters a = b = 105, c = 149 Å and one subunit in the asymmetric unit, corresponding to a packing density of 2.6 Å3 Da−1. The crystals diffract X-rays to at least 1.8 Å resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the key determinations of catalytic activity of this class of enzymes, for which no structures are currently available.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900014918
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  • 8
    Electronic Resource
    Electronic Resource
    Calcium nitride (Ca2N), a redetermination (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. i6-i7 
    Details
    ISSN: 1600-5368
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Ca2N adopts the anti-CdCl2 structure in which two sheets of calcium ions enclose a sheet of N3− ions, with each calcium bonded to three N3− at 2.4500 (3) Å and each nitrogen octahedrally coordinated by six calciums. Within one calcium sheet, each metal has three others at 3.2944 (8) Å and a further six at 3.6271 (3) Å. The distance between two calcium layers with no intervening nitrogen layer is 4.3221 (6) Å, and this intervening region contains no observable electron density. Neutron and X-ray powder diffraction studies have shown that the c-axis dimension changes with the synthetic method employed. In the single-crystal, c is significantly lower, reflecting the higher temperature employed in its formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S1600536801000472
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  • 9
    Electronic Resource
    Electronic Resource
    2′-Amino-3′,5′-dibromoacetophenone (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. o538-o539 
    Details
    ISSN: 1600-5368
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The synthesis and structure of a di-brominated derivative of 2′-aminoacetophenone, C8H7Br2NO, is described. The conformation observed in the solid state was found to be the same as that previously proposed for solution conformations of related compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S1600536801008388
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  • 10
    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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