Developing serial crystallography for room temperature structure & dynamics. This project aims to uncover the molecular structural dynamics of a bacterial enzyme responsible for protein folding in bacteria. This project expects to generate new knowledge to guide the development of a new type of antibacterial to circumvent antibiotic resistance. Expected outcomes of this project include new experimental, computational and simulation tools for dynamic X-ray crystallography including new capabiliti ....Developing serial crystallography for room temperature structure & dynamics. This project aims to uncover the molecular structural dynamics of a bacterial enzyme responsible for protein folding in bacteria. This project expects to generate new knowledge to guide the development of a new type of antibacterial to circumvent antibiotic resistance. Expected outcomes of this project include new experimental, computational and simulation tools for dynamic X-ray crystallography including new capabilities at the Australian Synchrotron for very small microcrystals of any biomolecule. This would provide a powerful new tool for the Australian structural biology community that should accelerate fundamental discoveries, including facilitating high-resolution structure determination of membrane proteins and drug development.Read moreRead less
Extending X-ray Crystallography to Allow Structure Retrieval from Highly Disordered Crystals and Nanocrystals. X-ray crystallography is one of the most important tools in structural biology, responsible for over 80 per cent of the protein structures solved today. Obtaining X-ray diffraction data however is critically dependent on having large, high quality crystals. Many proteins, particularly membrane proteins, only form nanocrystals or crystals of poor quality which prevents their structure be ....Extending X-ray Crystallography to Allow Structure Retrieval from Highly Disordered Crystals and Nanocrystals. X-ray crystallography is one of the most important tools in structural biology, responsible for over 80 per cent of the protein structures solved today. Obtaining X-ray diffraction data however is critically dependent on having large, high quality crystals. Many proteins, particularly membrane proteins, only form nanocrystals or crystals of poor quality which prevents their structure being solved. This project aims to combine ideas from X-ray coherent diffraction imaging and X-ray crystallography to develop a method that can be used for structure retrieval from nanocrystals or crystals which are highly disordered. A particular emphasis will be placed on solving the structure of membrane proteins which are of special importance in drug development.Read moreRead less