Crystallography, Structure and Function of Biological Macromolecules :

macrom5The MACROM group works in the area of understanding the three-dimensional structure of biomolecules by using single-crystal X-ray diffraction techniques to study the structure of DNA and its interactions with drugs, ions and proteins.

This group uses two complementary methodologies: crystallography and recombinant DNA techniques.

Crystallography studies require the molecules to be crystallized from extremely pure samples. The best crystals are selected using an optical microscope and are frozen with liquid nitrogen.

X-ray diffraction of these crystals is carried out in the ALBA synchrotron, keeping the crystlas under a continuous supply of liquid nitrogen. The diffraction obtained is processed with the aid of specific programs in order to determine the 3-D structure of the study sample. This method has been used to study a large number of synthetic oligonucleotides, which have provided valuable information on new forms of DNA (Hoogsteen, recombinant-like, superhelixes, etc.). Our research is readily applicable to areas such as pharmaceuticals, medicine and obtaining new materials and nanotechnology.

macrom6We also study the structure and function of different proteins that interact directly or indirectly with DNA. These studies require large quantities of pure protein. To this end, we incorporated recombinant DNA technology into our group in 1998. In this aspect, we have both the experience and the equipment needed for cloning and expressing proteins in prokaryotes and for purifying them and resolving their structure using x-ray diffraction. Furthermore, using directed mutagenesis techniques it is possible to obtain recombinant forms designed both to improve their crystallization and to study specific functional aspects.  

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