Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/96106
Title: Crystallization and diffraction of single-crystals at ALBA Synchrotron to structure determination of a Relaxase protein
Other Titles: Cristal•lització i difracció de monocristalls al Sincrotró ALBA per a la determinació estructural d’una proteïna Relaxassa
Author: Guevara Puig, Tibisay
Director: Sainz García, Daniel
Boer, Roeland
Keywords: Sincrotrons
Cristal·lització
Proteïnes
Tesis
Synchrotrons
Crystallization
Proteins
Theses
Issue Date: 11-Jan-2016
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
Note: Treballs Finals de Grau de Química, Facultat de Química, Universitat de Barcelona, Any: 2016, Tutor: Daniel Sainz García i Roeland Boer
URI: http://hdl.handle.net/2445/96106
Appears in Collections:Treballs Finals de Grau (TFG) - Química

Files in This Item:
File Description SizeFormat 
TFG_QU_Guevara.pdf1.65 MBAdobe PDFView/Open


This item is licensed under a Creative Commons License Creative Commons