ARCIMBOLDO-SX

• Applicant: Dr. Kathrin Meindl
• Subject Area: Structural Biology
• Term: from 2010 to 2011
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 174923832

X-ray crystallography serves as an important tool to investigate the molecular structure of many chemical compounds. Knowing the exact structure is essential to understand the mechanism of reactions. Also, atomic radii, bond lengths and the bonding situation in molecules are determined with the help of X-ray crystallography. Getting a detailed knowledge of the structural situation of a molecule is especially important for macromolecules when information about activity or the mechanism for recognition and binding of substrates is investigated. This helps to show how pharmaceuticals interact with their targets and how the structure can be modified to improve this interaction. However, macromolecular crystallography is computationally intensive. In the present project I intend to exploit the increasing computer power to tackle the crystallographic phase problem. The ultimate goal of the proposal is to develop a supercomputer version, remotely controlled over a web server, of the ab initio crystallographic phasing program ARCIMBOLDO (http://dx.doi.org/10.1038/nmeth.1365), which performs parallel model fragment search with the program PHASER coupled to density modification with the program SHELXE. This method has been successfully used for ab initio solution at 2 Å of a previously unknown protein with 222 residues in the asymmetric unit and no heavy atoms present.

• DFG Programme: Research Fellowships
• International Connection: Spain
• Host: Professorin Dr. Isabel Usón