Acta Cryst. (2000). B56, 690-696 [doi:10.1107/S0108768100002202]
Abstract: The crystal structures of complexes of maleic acid with L-histidine and L-lysine have been determined. The two crystallographically independent amino acid molecules in the L-histidine complex have different closed conformations, while the lysine molecule in its complex has the most favourable conformation sterically with an all-trans sidechain trans to the ![[alpha]](/logos/entities/alpha_rmgif.gif)
-carboxylate group. The maleic acid molecules exist as semi-maleate ions of similar conformation and contain a symmetric O
HO hydrogen bond. Amino acid cations and semi-maleate anions aggregate into alternate layers in both the structures. The arrangement of molecules in the histidine layer in L-histidine semi-maleate is closer to that in the crystals of the free amino acid than in other L-histidine complexes. On the other hand, the arrangement of lysine molecules in its semi-maleate complex is different from any observed so far. However, the well established characteristic interaction patterns involving amino and carboxylate groups still play a major role in holding the molecules together in the crystal of the complex.
Online 1 August 2000
 |   Structure factor file (CIF format) (69.6 kbytes) |
| Structure factor file (CIF format) (51.6 kbytes) |
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