Reflections on the Many Facets of Protein Microcrystallography
Marion Boudes A B , Damià Garriga A B and Fasséli Coulibaly A C
+ Author Affiliations
- Author Affiliations
A School of Biomedical Sciences, Monash University, Clayton, Vic. 3168, Australia.
B These authors contributed equally to this work.
C Corresponding author. Email: fasseli.coulibaly@monash.edu
Dr Marion Boudes received her M.Sc. from Montpellier SupAgro in 2008 and graduated with her Ph.D. from the University of Paris-Sud in 2011. She subsequently joined the Structural Virology laboratory in Monash University as a post-doctoral researcher. |
Dr Damià Garriga obtained his Ph.D. degree in health and life sciences from the Pompeu Fabra University in Barcelona in 2010. He worked as a researcher in the Spanish Research Council until 2013, when he moved to Australia to join the Structural Virology laboratory at Monash University, where he is currently working as a senior research fellow. |
Dr Fasséli Coulibaly is a structural biologist whose work focuses on the architecture and function of large macromolecular assemblies. He graduated with a Ph.D. in protein crystallography from the University of Paris-Sud in 2003 and, after holding a post-doctoral position at the University of Auckland, established the Structural Virology laboratory at Monash University in 2008. His current research interests include the assembly, replication, and evolution of viruses as well as the design of new approaches for vaccination. |
Australian Journal of Chemistry 67(12) 1793-1806 https://doi.org/10.1071/CH14455
Submitted: 18 July 2014 Accepted: 2 September 2014 Published: 24 October 2014
Abstract
The use of X-ray crystallography for the structure determination of biological macromolecules has experienced a steady expansion over the last 20 years with the Protein Data Bank growing from <1000 deposited structures in 1992 to >100 000 in 2014. The large number of structures determined each year not only reflects the impact of X-ray crystallography on many disciplines in the biological and medical fields but also its accessibility to non-expert laboratories. Thus protein crystallography is now largely a mainstream research technique and is routinely integrated in high-throughput pipelines such as structural genomics projects and structure-based drug design. Yet, significant frontiers remain that continuously require methodological developments. In particular, membrane proteins, large assemblies, and proteins from scarce natural sources still represent challenging targets for which obtaining the large diffracting crystals required for classical crystallography is often difficult. These limitations have fostered the emergence of microcrystallography, novel approaches in structural biology that collectively aim at determining structures from the smallest crystals. Here, we review the state of the art of macromolecular microcrystallography and recent progress achieved in this field.
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