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  • Springer  (30)
  • Oxford University Press  (17)
  • International Union of Crystallography (IUCr)  (14)
  • American Institute of Physics (AIP)  (7)
  • 2000-2004  (48)
  • 1965-1969  (20)
  • 1955-1959
  • 2001  (48)
  • 1967  (20)
Collection
Publisher
Years
  • 2000-2004  (48)
  • 1965-1969  (20)
  • 1955-1959
Year
  • 11
    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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  • 12
    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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  • 13
    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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  • 14
    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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  • 15
    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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  • 16
    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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  • 17
    Electronic Resource
    Electronic Resource
    2′-Amino-5′-bromoacetophenone (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. o540-o541 
    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 brominated derivative of 2′-aminoacetophenone, C8H8BrNO, is described. The conformation observed in the solid state was found to be the same as that previously determined by NMR studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S160053680100839X
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  • 18
    Electronic Resource
    Electronic Resource
    The structure and domain organization of Escherichia coli isocitrate lyase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1209-1218 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 Å resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901008642
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  • 19
    Electronic Resource
    Electronic Resource
    Cloning, purification, crystallization and preliminary crystallographic analysis of Bacillus subtilis LuxS (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1324-1325 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: LuxS of Bacillus subtilis is a member of a novel family of proteins with a potential role in quorum sensing, controlling important aspects of cellular physiology in a range of microbial species. B. subtilis luxS was cloned, expressed in Escherichia coli, purified and crystallized using the hanging-drop method of vapour diffusion with ammonium sulfate as the precipitant. The crystals belong to one of the enantiomorphic space groups P6122 or P6522, with approximate unit-cell parameters a = b = 63.6, c = 151.5 Å and one subunit in the asymmetric unit, corresponding to a packing density of 2.5 Å3 Da−1. The crystals diffract X-rays to at least 1.55 Å resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the key determinants of function of this class of proteins, for which no structures are currently available.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901011611
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  • 20
    Electronic Resource
    Electronic Resource
    LISA: an intranet-based flexible database for protein crystallography project management (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1341-1343 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The increase in the number of projects carried out in protein crystallography laboratories has emphasized the need for effective management of project information and data. To meet this need, a flexible web-accessible database for protein crystallography project management (LISA) has been developed using the open-source software MySQL and PHP4. The database contains information about all aspects of structure-determination projects, including primer and plasmid sequences, protein expression, purification and crystallization results, structure coordinate files and resultant publications. The database web pages include links to relevant servers and contain, in addition, tools for processing stored information. The software package is freely available.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901009295
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