Evidence from x-ray absorption fine structure spectroscopy for significant differences in the structure of concanavalin A in solution and in the crystal
- 17 April 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (15) , 3599-3603
- https://doi.org/10.1021/bi00467a002
Abstract
We have used X-ray absorption fine structure spectroscopy (XAFS) to study and compare the structure of concanavalin A in crystals and in aqueous solution. Significant differences were found between crystal and solution in the configuration of the transition-metal site of the protein. The metal has six ligands in solution but only five in the crystal. The ligand bond lengths are shorter in the crystal than in solution. The vibrational disorder in the crystal and possibly the corresponding bond length show a negative temperature dependence whereas in solution they vary normally with temperature. The anomalous temperature dependence in the crystal suggests that as the temperature decreases the protein molecules are subject to additional stresses, which are transmitted as a tensile stress at the metal site leading to distorted geometry and lengthening and weakening of metal-ligand bonds.This publication has 2 references indexed in Scilit:
- Manganese and calcium binding sites of concanavalin AJournal of Molecular Biology, 1982
- Modelling the unusual temperature dependence of atomic displacements in proteins by local nonharmonic potentials.Proceedings of the National Academy of Sciences, 1981