Open AccessRevisiting glutaraldehyde cross‐linking: the case of the Arg–Lys intermolecular doublet
Author(s) -
Salem Michèle,
Mauguen Yves,
Prangé Thierry
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109054037
Subject(s) - glutaraldehyde , lysine , chemistry , cross link , intermolecular force , polymerization , monomer , crystallography , protein crystallization , side chain , polymer chemistry , polymer , biochemistry , molecule , organic chemistry , amino acid , crystallization
In addition to the common use of glutaraldehyde to nonspecifically cross‐link protein crystals through lysine residues disposed on the surface of the protein, the use of gentle vapour diffusion of glutaraldehyde offers a convenient way to limit polymerization and to allow slow diffusion throughout the crystal. In the case of trimeric barnase crystals, a specific cross‐link was observed between an lysine side chain and an arginine side chain that were spatially disposed at the ideal distance on the protein surface in the three monomers. Here, the direct observation of a specific Lys–Arg cross‐link site is reported and a mechanism is proposed for the reaction.