The pendant-arm macrocycle, meso-5,5,7,12,12,14-hexamethyl-1,4,8,11tetraazacyclotetradecane-1,8-di-(1-methylnaphthalene) has been synthesized and its single crystal structure determined. The molecule crystallizes in a primitive monoclinic cell, with the space group P21/a (#14). The cell dimensions are a = 10.778(3)Å, b = 13.809(3) Å, c = 11.420(2) Å, ∃ = 102.49(2)°, volume = 1659.5(6) Å.

In the title compound, C16H12N2O3, the 2H-chromene moiety is essentially planar, with an r.m.s. deviation of the nine constituent atoms from the mean plane of 0.0093 Å, and makes a dihedral angle of 76.84 (3)° with the pendant phenyl ring. An intra-molecular N-H⋯O hydrogen bond helps to determine the conformation of the side chain. In the crystal, N-H⋯O and N-H⋯N hydrogen bonds link the mol-ecu...

From conformational analysis, we have determined the two lowest energy crystal structures for the hard segments of 4,49-diphenylmethane diisocyanate/1,4butanediol (MDI/BDO)-based polyurethane elastomer. Both crystal forms give prominent X-ray scattering at ;7.6 Å. In one crystal form, (1), there is strong hydrogen bonding between linear chains with a density of 1.30 g/cm, while in the other for...

the crystal structure of the title schiff base complex is obtained by single-crystal x-ray diffraction data.the solid state structure determination reveals that the coordination geometry around the copper(ii) center istetrahedrally distorted square-planar. the crystal packing shows one dimensional infinite chains which arisesfrom the intermolecular interaction and stabilize the crystal packing.

The three-dimensional structures of D-Phe-Pro-Arg-chloromethyl ketone-inhibited thrombin in complex with Tyr-63-sulfated hirudin (ternary complex) and of thrombin in complex with the bifunctional inhibitor D-Phe-Pro-Arg-Pro-(Gly)4-hirudin (CGP 50,856, binary complex) have been determined by X-ray crystallography in crystal forms different from those described by Skrzypczak-Jankun et al. (Skrzyp...

Omp32, the strongly anion-selective porin from Comamonas acidovorans, has been crystallized. Two crystal forms were observed, both of which belong to space group R3, but exhibit different cell dimensions a = b = 106.7, c = 140.6 A (crystal form I) and a = b = 87.1, c = 135.3 A (crystal form II) with one trimer per asymmetric unit. The crystals diffract to 2.2 and 2.3 A resolution, respectively....

An amino-terminal fragment of human apolipoprotein E3 (residues 1-165) has been expressed and crystallized in three different crystal forms under similar crystallization conditions. One crystal form has nearly identical cell dimensions to the previously reported orthorhombic (P2(1)2(1)2(1)) crystal form of the amino-terminal 22 kDa fragment of apolipoprotein E (residues 1-191). A second orthorh...