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  • 1
    Electronic Resource
    Electronic Resource
    Alaninyltryptophan hydrate, glycyltryptophan dihydrate and tryptophylglycine hydrate (2000)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. e469-e471 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structures of the title tryptophan-containing dipeptides, C14H17N3O3·H2O, (I), C13H15N3O3·2H2O, (II), and C13H15N3O3·H2O, (III), respectively, contain at least one water molecule of solvation. As a result, the crystal packing of these compounds is composed of regions of water-mediated hydrogen bonding and tryptophan ring-to-ring stacking separated by the length of the molecule. The tryptophan rings stack in a continuous layer that, when viewed edge-on from the outermost part of the tryptophan ring, exhibits a herring-bone motif. However, owing to the lack of direct overlap of adjacent rings, no degree of π contact or long-range delocalization of ring systems is possible here. The overall molecular conformations of (I) and (III) contain a folding of one peptide over the other, such that a minimum in molecular volume occurs without any intramolecular hydrogen bonding. In these two dipeptides, extensive hydrogen bonding is observed to and from the single water molecule of solvation. In the crystal structure of (II), however, an extended molecule conformation complements a more extensive hydrogen-bonding scheme involving two water molecules of solvation per dipeptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270100011926
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Synchrotron X-ray reciprocal-space mapping, topography and diffraction resolution studies of macromolecular crystal quality (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 868-880 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A comprehensive study of microgravity and ground-grown chicken egg-white lysozyme crystals is presented using synchrotron X-ray reciprocal-space mapping, topography techniques and diffraction resolution. Microgravity crystals displayed reduced intrinsic mosaicities on average, but no differences in terms of strain over their ground-grown counterparts. Topographic analysis revealed that in the microgravity case the majority of the crystal was contributing to the peak of the reflection at the appropriate Bragg angle. In the ground-control case only a small volume of the crystal contributed to the intensity at the diffraction peak. The techniques prove to be highly complementary, with the reciprocal-space mapping providing a quantitative measure of the crystal mosaicity and strain (or variation in lattice spacing) and the topography providing a qualitative overall assessment of the crystal in terms of its X-ray diffraction properties. Structural data collection was also carried out at the synchrotron.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900005837
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  • 4
    Electronic Resource
    Electronic Resource
    X-LIGAND: an application for the automated addition of flexible ligands into electron density (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 696-705 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: With the advent of drug-design experiments where the interaction between a protein and a ligand is determined using X-ray crystallography, the use of automated methods for modelling the ligand into electron density represents a powerful tool. Once the protein structure has been determined by crystallography it is normal that subsequent ligand-complex structures are isomorphous, or nearly so, with the original structure and it is necessary only to determine the fit of ligand to any unsatisfied electron density. The X-LIGAND application was designed with this protocol in mind and provides a tool that searches for unsatisfied electron density and then fits flexible ligands to this within minutes without user intervention.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901003894
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  • 5
    Electronic Resource
    Electronic Resource
    Location of Zn within the Mg12(LaxCe1−x) lattice by X-ray incoherent channelling patterns (2001)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 321-332 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Systematic electron diffraction studies on intermetallic precipitates formed within a lightweight Mg–RE–Zn alloy (RE = La or Ce) identify these to be of structural type Mn12Th (space group I4/mmm). Analytical electron microscopy yields an overall composition of Mg12(LaxCe1−x) with x ̃0.43, with 1 at.% Zn incorporated within the lattice. Variations in characteristic X-ray emission rates, as an electron beam is rocked near zone-axis orientations, are used to form two-dimensional channelling patterns, termed X-ray incoherent channelling patterns. This channelling contrast enables a specific sublattice site that is occupied by Zn to be unambiguously identified within the Mg12RE lattice. The particular sublattice site is denoted by the Wyckoff letter f, and is one of the three different Mg sublattice sites f, i and j. Of these three sites, the Wigner–Seitz cell that is centred on the f sublattice site has the largest Mg–RE interatomic distance, and therefore the f site is expected to be favoured for accommodating the substitution of a larger Zn atom.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108767300019577
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  • 6
    Electronic Resource
    Electronic Resource
    Creating structure features by data mining the PDB to use as molecular-replacement models (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1421-1427 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Mathematical data-mining techniques to generate a representative set of protein fragments are described. Protein fragments are used as search models within the macromolecular phasing method of molecular replacement to attempt to phase protein data without a homologous model correctly. Preliminary investigations using these fragments indicate that molecular replacement with AMoRe is not sensitive enough to phase myoglobin or insulin data sufficiently for successful refinement. The results suggest that more advanced molecular replacement techniques may be successful, though at present these are not computationally practical.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012483
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate dehydrogenase from Corynrbacterium glutamicum. Erratum (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1512-1512 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: In the paper by Audette et al. [Acta Cryst. (1999), D55, 1584–1585] the postal code of one of the authors was printed incorrectly. The correct version is given above. Also the reaction catalyzed by isocitrate dehydrogenase was given incorrectly in the paper; the correct reaction is given below.\eqalign {{\rm Isocitrate} + {\rm NADP}^{+} & \,\, \longleftrightarrow \,\, {\rm Oxalosuccinate} + {\rm NADPH} \cr {\rm Oxalosuccinate} & \,\,\longleftrightarrow\,\, \alpha{\rm-Ketoglutarate} + {\rm CO}_{2}}.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900013640
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of H defects in the aluminium–hydrogen system using small-angle scattering techniques (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 34 (2001), S. 119-129 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Aluminium foils (99.99% purity) and single crystals (99.999% purity) were charged with hydrogen using a gas plasma method and electrochemical methods, resulting in the introduction of a large amount of hydrogen. X-ray diffraction measurements indicated that within experimental error there was a zero change in lattice parameter after plasma charging. This result is contradictory to almost all other face-centred cubic (f.c.c.) materials, which exhibit a lattice expansion when the hydrogen enters the lattice interstitially. It is hypothesized that the hydrogen does not enter the lattice as an interstitial solute, but instead forms an H–vacancy complex at the surface that diffuses into the volume and then clusters to form H2 bubbles. Small- and ultra-small-angle neutron scattering (SANS, USANS) and small-angle X-ray scattering (SAXS) were primarily employed to study the nature and agglomeration of the H–vacancy complexes in the Al–H system. The SAXS results were ambiguous owing to double Bragg scattering, but the SANS and USANS investigation, coupled with results from inelastic neutron scattering, and transmission and scanning electron microscopy, revealed the existence of a large size distribution of hydrogen bubbles on the surface and in the bulk of the Al–H system. The relative change in lattice parameter is calculated from the pressure in a bubble of average volume and is compared with the experimentally determined value.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889800018239
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  • 9
    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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