Related Experiment Video
Updated: Aug 23, 2026
Synthesis of 1,2-Azaborines and the Preparation of Their Protein Complexes with T4 Lysozyme Mutants
Published on: March 25, 2017
Crystallization and preliminary X-ray analysis of bacteriophage lambda lysozyme in which all tryptophans have been
C Evrard1, J P Declercq, J Fastrez
1Laboratoire de Chimie Physique et de Cristallographie, Université Catholique de Louvain, Louvain-La-Neuve, Belgium. delercq@cpmc.ucl.ac.be
Abstract:
After many unsuccessful attempts to crystallize the bacteriophage lambda lysozyme, a mutant where all the tryptophan residues have been replaced by aza-tryptophans has been crystallized by the vapor-diffusion method. The crystals are orthorhombic and belong to space group P2(1)2(1)2(1) with cell dimensions a = 73.01, b = 78.80, c = 82.31 A. Diffraction data were collected using synchrotron radiation sources. Crystals diffract to a resolution of 2.3 A. Data from two different platinum derivatives were also recorded to 2.8 and 2.5 A, respectively.
