Auxeticity in nano/microtubes produced from orthorhombic crystals

2016 ◽  
Vol 25 (5) ◽  
pp. 054006 ◽  
Author(s):  
Robert V Goldstein ◽  
Valentin A Gorodtsov ◽  
Dmitry S Lisovenko ◽  
Mikhail A Volkov
Author(s):  
Tadashi Ishida

AbstractA method has been proposed for indexing powder diffraction patterns using a new criterion. An improved version of our previous procedure (Ishida and Watanabe, 1982) is proposed especially for determining the monoclinic unique axis, crystallographic axes of orthorhombic crystals and


Author(s):  
Mariot Breitwieser ◽  
Siegfried Göttlicher ◽  
Helmut Paulus

AbstractOrthorhombic crystals of nearly 1 cm lengths have been obtained from a solution of cadmiumbenzohydroxamate in ethylenediamine. The space group is


Author(s):  
L. G. Berry

Jamesonite is described in Dana (1892, p. 122) as a soft, brittle, steel-grey to lead-grey mineral forming acicular orthorhombic crystals, a: b = ‘0·915:1’ (in error for 0·8195:1), with perfect basal cleavage; composition, 2PbS.Sb2S3; principal occurrence, Cornwall. Jamesonite is taken as the type member of a group that includes cosalite, described in the first of these studies (1939), dufrenoysite, and other minerals of analogous composition.


Author(s):  
R. H. Solly

Professor Baumhauer, in January, 1901, described five very small crystals of a new mineral, to which he gave the name seligmannite. They were associated with rathite and binnite in dolomite, and came from the Lengenbach quarries in the Binnenthal, Switzerland. In June, 1902, he described another crystal, the angles of which agreed fairly well with those of the crystals he had previously measured. In habit and twinning, these orthorhombic crystals so closely resembled bournonite that he ventured to assign to the new mineral the chemical formula Cu2S.2PbS.As2S3, but from paucity of material he was unable to make a chemical analysis.


Myoglobin of Physeter catodon (sperm whale) forms monoclinic crystals with space group P 2 1 (type A ) in ammonium sulphate, and orthorhombic crystals with space group P 2 1 2 1 2 1 (type B ) in phosphate. Almost identical crystal forms are obtained from related species of whale. Two-dimensional Patterson projections have been computed from some principal zones of reflexions in each type of crystal. They are used to derive the chain directions of the poly­peptide chains in the molecules relative to the crystal axes, and to suggest plausible methods of packing in the two forms. The data are best fitted by a molecule having dimensions about 25 x 34 x 42 Å, the latter dimension being parallel to the chain direction. Measurements of electron-spin resonance (Bennett & Ingram 1956) and of optical dichroism have been used to determine the orientation of the planes of the haem group and the angle between them and the chains. It is concluded that the angle is 40 to 50° in the two forms, in good agreement with the value found for type F crystals in an earlier paper, namely, 41°. Thus in all three crystal types A , B and F the data are consistent with the molecule having the same set of dimensions, associated with a common chain direction and a common relation between chain direction and haem group.


1999 ◽  
Vol 55 (12) ◽  
pp. 2043-2046 ◽  
Author(s):  
Marie-France Giraud ◽  
Helen J. McMiken ◽  
Gordon A. Leonard ◽  
Paul Messner ◽  
Chris Whitfield ◽  
...  

L-Rhamnose is an essential component of the cell wall of many pathogenic bacteria. Its precursor, dTDP-L-rhamnose, is synthesized from α-D-glucose-1-phosphate and dTTP via a pathway requiring four distinct enzymes: RmlA, RmlB, RmlC and RmlD. RmlD catalyses the terminal step of this pathway by converting dTDP-6-deoxy-L-lyxo-4-hexulose to dTDP-L-rhamnose. RmlD from Salmonella enterica serovar Typhimurium has been overexpressed in Escherichia coli. The recombinant protein was purified by a two-step protocol involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated that the recombinant protein is monodisperse. Crystals of native and selenomethionine-enriched RmlD have been obtained using the sitting-drop vapour-diffusion method with polyethylene glycol as precipitant. Diffraction data have been collected from orthorhombic crystals of both native and selenomethionyl-derivatized protein, allowing tracing of the protein structure.


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