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16 citations found for Watson, A.

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The YncE protein of E. coli has been overproduced and purified and preliminary crystallographic analysis has been performed to 2.1 Å resolution. The structure reveals a seven-bladed β-propeller fold.

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Crystallization of the proposed FAD-containing ferri-siderophore reductase protein YqjH from E. coli has been performed and the structure has been determined to 3.0 Å resolution. The structure shows similarity to another proposed siderophore-interacting protein from S. putrefaciens and weak similarity to members of the NAD(P)H:flavin oxidoreductase superfamily.

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The crystallization and structure determination of the apo form of a novel haem-containing Tat substrate, YcdB from E. coli, has been solved to 2.0 Å resolution. The preliminary structure shows similarity to other haem-dependent peroxidases, despite low sequence homology.

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The title compound, [PtCl2(C14H16)], contains a square-planar d8 platinum(II) center which is coordinated by two Cl atoms and the double bonds of a rigid polycyclic ligand containing a 1,4-cyclo­octa­diene subunit. This compound is an inter­esting substrate for additional mechanistic studies of catalytically active metal complexes.

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Acta Cryst. (2000). A56, s95
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Acta Cryst. (2023). A79, C1041
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N-Acetylneuraminate lyase, an enzyme involved in the bacterial uptake and metabolism of sialic acid, is a promising target for antibiotic development against pathogenic bacteria. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of N-acetylneuraminate lyase from methicillin-resistant S. aureus to 1.70 Å resolution are reported.

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis to 1.84 Å resolution of N-acetylmannosamine-6-phosphate 2-epimerase from methicillin-resistant S. aureus, an enzyme involved in the catabolism of sialic acid and a novel antimicrobial drug target, are reported.

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The surface chemistry of the wings of the Clanger cicada Psaltoda claripennis has been studied using two synchrotron infrared beamlines. A heterogeneous surface distribution of long-chain hydrocarbons has been observed, which can account for this insect wing's previously observed heterogeneous superhydrophobicity, and which will assist in further understanding the structure and function of similar insect wings.

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Recombinant human CLEC-2 was crystallized in the orthorhombic space group P212121 and X-ray diffraction data were collected to 2.0 Å.

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Recombinant human CLEC5A was crystallized in the trigonal space group P31 and X-ray diffraction data were collected to 1.56 Å resolution.

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The title compound, C22H22Si, is a benzosilacyclo­pentene in which the silacyclo­pentene ring assumes an envelope conformation. The Si atom is displaced by 0.722 (4) Å from the mean plane of the four C atoms, and is bonded to two methyl groups and to two Csp3 atoms in the silacyclo­pentene ring. One phenyl ring is attached to each of these two C atoms in a cis configuration. The Si atom and the two methyl groups lie on a crystallographic mirror plane which relates the two halves of the molecule. The average Si-Cmeth­yl bond distance is 1.852 (3) Å. The Si-Csp3 bond distance is 1.886 (2) Å, and the corresponding Csp3-Si-Csp3 angle is 93.0 (1)°. The displacement ellipsoids for the atoms in the fused benzene ring suggest a probable disorder, but no satisfactory disorder model could be found.

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The title compound, C18H6Cl12O2, is a valuable precursor for the synthesis of mol­ecular tweezers. These tweezers require a tether part and two pincer units with syn orientation that can create a cavity large enough to include suitable guest compounds by noncovalent inter­action. The title compound is an ideal tether unit with syn-oriented double bonds, a π–π distance of 6.28 (1) Å, and the relative ease of functionalization of the two dichloro­ethene subunits.

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Acta Cryst. (1996). A52, C250
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Several glucose analogue inhibitors of glycogen phosphorylase have been studied in crystallographic, kinetic and 3D QSAR experiments. Comparison of the N-methylacetylglucopyranosyl amine with the analogous C-methylamide derivative showed a fivetold improvement in Ki and a 200-fold improvement compared with glucose.

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