Crystallization and diffraction of single-crystals at ALBA Synchrotron to structure determination of a Relaxase protein

Abstract

The aim of the present work is the structure description of two variant (full length and Nterminal) of a protein with Relaxase activity. Both pure variants were crystallized using sitting drop vapor diffusion technique. Crystals obtained were optimized increasing its quality and some of them were treated to derivatize it with metals. Diffraction of crystals and pre-treatment of protein were integrally performed in ALBA Synchrotron (Barcelona) installations. In BL-13 XALOC beamline were collected the data which were processed and evaluated as good quality data. The phase problem solution was not possible by applying Molecular Replacement nor detecting the anomalous signal of derivatives crystals. The lack of phases did not permit to solve the electron density equation, and therefore, it was not possible to complete the model building