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• W2010588887 abstract "The crystal structure of a glycopeptide antibiotic A–40926 aglycone was investigated by X-ray analysis at −120°. A-40926 crystallises in the orthorhombic space group P212121 with two monomers in the asymmetric unit, a = 21.774(4), b = 28.603(7), c = 29.757(4) Å. ‘Conventional’ direct methods approach failed to solve the structure, but a novel iterative real/reciprocal space procedure was successful. Refinement against 11248 F2 data led to R1 = 13.3% for 6770 F > 4σ (F). The two monomers of A-40926 have similar conformations and are bound by antiparallel H-bonds to form a ‘chain’ structure of connecting dimers. The antibiotic molecule possesses a ‘binding pocket’ for the C-terminal carboxy group of the cell-wall protein, which is consisten with suggestions based on NMR data and the recently reported crystal structure of ureido-balhimycin. In A-40926 the monomers are polymerically linked by H-bonds, quite unlike the tight dimer formation observed in ureido-balhimycin." @default.
• W2010588887 created "2016-06-24" @default.
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• W2010588887 date "1996-10-30" @default.
• W2010588887 modified "2023-10-17" @default.
• W2010588887 title "The Molecular and Crystal Structure of the Glycopeptide A-40926 Aglycone" @default.
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• W2010588887 doi "https://doi.org/10.1002/hlca.19960790714" @default.
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