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Updated: Jan 21, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
N-[2-(Tri-fluoro-meth-yl)phen-yl]maleamic acid: crystal structure and Hirshfeld surface analysis
P A Suchetan1, Shet M Prakash1, N K Lokanath2
1Dept. of Chemistry, University College of Science, Tumkur University, Tumkur, 572 103, India.
Abstract:
The title mol-ecule, C11H8F3NO3, adopts a cis configuration across the -C=C- double bond in the side chain and the dihedral angle between the phenyl ring and side chain is 47.35 (1)°. The -COOH group adopts a syn conformation (O=C-O-H = 0°), unlike the anti conformation observed in related maleamic acids. In the crystal, inversion dimers linked by pairs of O-H⋯O hydrogen bonds are connected via N-H⋯O hydrogen bonds and C-H⋯O inter-actions into (100) sheets, which are cross-linked by another C-H⋯O inter-action to result in a three-dimensional network. The Hirshfeld surface fingerprint plots show that the highest contribution to surface contacts arises from O⋯H/H⋯O contacts (26.5%) followed by H⋯F/F⋯H (23.4%) and H⋯H (17.3%).
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