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Triclinic Crystal (triclinic + crystal)

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Chemistry100%

Terms modified by Triclinic Crystal

  • triclinic crystal system
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    Selected Abstracts

    Phase transition of triclinic hen egg-white lysozyme crystal associated with sodium binding

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2004
    Kazuaki Harata
    A triclinic crystal of hen egg-white lysozyme obtained from a D2O solution at 313,K was transformed into a new triclinic crystal by slow release of solvent under a temperature-regulated nitrogen-gas stream. The progress of the transition was monitored by X-ray diffraction. The transition started with the appearance of strong diffuse streaks. The diffraction spots gradually fused and faded with the emergence of diffraction from the new lattice; the scattering power of the crystal fell to a resolution of 1.5,Å from the initial 0.9,Å resolution. At the end of the transition, the diffuse streaks disappeared and the scattering power recovered to 1.1,Å resolution. The transformed crystal contained two independent molecules and the solvent content had decreased to 18% from the 32% solvent content of the native crystal. The structure was determined at 1.1,Å resolution and compared with the native structure refined at the same resolution. The backbone structures of the two molecules in the transformed crystal were superimposed on the native structure with root-mean-square deviations of 0.71 and 0.96,Å. A prominent structural difference was observed in the loop region of residues Ser60,Leu75. In the native crystal, a water molecule located at the centre of this helical loop forms hydrogen bonds to main-chain peptide groups. In the transformed crystal, this water molecule is replaced by a sodium ion with octahedral coordination that involves water molecules and a nitrate ion. The peptide group connecting Arg73 and Asn74 is rotated by 180° so that the CO group of Arg73 can coordinate to the sodium ion. The change in the X-ray diffraction pattern during the phase transition suggests that the transition proceeds at the microcrystal level. A mechanism is proposed for the crystal transformation. [source]

    Two polymorphs of lysozyme nitrate: temperature dependence of their solubility

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 10-1 2002
    L. Legrand
    Two crystallographic forms of lysozyme nitrate are known, namely monoclinic and triclinic. Having previously determined the temperature dependence of the solubility of the monoclinic form (0.2 M NaNO3 solutions at pH = 4.5) [Legrand et al. (2001). J. Crystal Growth232, 244-249], we focus here on the solubility of the triclinic form. The temperature dependence of the solubility of this crystallographic form has been measured with a static light device developed in our laboratory. This device allows to observe of the dissolution of one phase and/or the occurrence of a new one by varying the temperature with a sweep rate as low as 0.6 degree/hour. The new solubility data are complemented with crystallographic data of the triclinic form for the sake of completeness. The faces of a triclinic crystal are indexed. The crystallisation enthalpy of the triclinic form is deduced from these new results. These new solubility data allow us now to discuss (1) the publishedprotocols used to obtain the monoclinic and triclinic forms of lysozyme nitrate and (2) the phase transformation. [source]

    A triclinic crystal form of Escherichia coli 4-diphosphocytidyl-2C -methyl- d -erythritol kinase and reassessment of the quaternary structure

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2010
    Justyna Kalinowska-T
    4-Diphosphocytidyl-2C -methyl- d -erythritol kinase (IspE; EC 2.7.1.148) contributes to the 1-deoxy- d -xylulose 5-phosphate or mevalonate-independent biosynthetic pathway that produces the isomers isopentenyl diphosphate and dimethylallyl diphosphate. These five-carbon compounds are the fundamental building blocks for the biosynthesis of isoprenoids. The mevalonate-independent pathway does not occur in humans, but is present and has been shown to be essential in many dangerous pathogens, i.e. Plasmodium species, which cause malaria, and Gram-negative bacteria. Thus, the enzymes involved in this pathway have attracted attention as potential drug targets. IspE produces 4-diphosphosphocytidyl-2C -methyl- d -erythritol 2-phosphate by ATP-dependent phosphorylation of 4-diphosphocytidyl-2C -methyl- d -erythritol. A triclinic crystal structure of the Escherichia coli IspE,ADP complex with two molecules in the asymmetric unit was determined at 2,Å resolution and compared with a monoclinic crystal form of a ternary complex of E. coli IspE also with two molecules in the asymmetric unit. The molecular packing is different in the two forms. In the asymmetric unit of the triclinic crystal form the substrate-binding sites of IspE are occluded by structural elements of the partner, suggesting that the `triclinic dimer' is an artefact of the crystal lattice. The surface area of interaction in the triclinic form is almost double that observed in the monoclinic form, implying that the dimeric assembly in the monoclinic form may also be an artifact of crystallization. [source]

    Radiation-induced site-specific damage of mercury derivatives: phasing and implications

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2005
    Udupi A. Ramagopal
    The behavior of mercury-derivatized triclinic crystals of a 60,kDa protein target from the New York Structural GenomiX Research Consortium provides novel insights into the mechanism of heavy-atom-specific radiation damage and its potential exploitation for de novo structure solution. Despite significant anomalous signal, structure solution by classic SAD and MAD phasing approaches was not successful. A detailed analysis revealed that significant isomorphic variation of the diffracted intensities was induced by X-ray irradiation. These intensity changes allowed the crystal structure to be solved by the radiation-damage-induced phasing (RIP) technique. Inspection of the crystal structure and electron-density maps demonstrated that the covalent S,­Hg bonds at all four derivatized cysteine sites were much more susceptible to radiation-induced cleavage than other bonds typically present in native proteins. A simple diagnostic is described to identify the fingerprint of such decay at the time of data collection/processing. The rapid radiation-induced decomposition of mercury adducts is consistent with the difficulties frequently associated with the experimental phasing of mercury derivatives and suggests a straightforward solution to overcome this limitation by radiation-damage-induced phasing with anomalous scattering (RIPAS). These results indicate that historically recalcitrant and newly emerging difficulties associated with Hg phasing should be revisited. [source]