Abstract
Over the past 20 years a variety of technological advances in X-ray crystallography have shortened the time required to determine the structures of large macromolecules (i.e., proteins and nucleic acids) from several years to several weeks or days. However, one of the remaining challenges is the ability to produce diffraction-quality crystals suitable for a detailed structural analysis. Although the development of automated crystallization systems combined with protein engineering (site-directed mutagenesis to enhance protein solubility and crystallization) have improved crystallization success rates, there remain hundreds of proteins that either cannot be crystallized or yield crystals of insufficient quality to support X-ray structure determination. In an attempt to address this bottleneck, an international group of scientists has explored use of a microgravity environment to crystallize macromolecules. This paper summarizes the history of this international initiative along with a description of some of the flight hardware systems and crystallization results.
Highlights
The use of X-ray crystallography to determine the structures of macromolecules has progressed markedly in recent years
The research was performed by group of international investigators who were sponsored by space agencies from several countries including the National Aeronautics and Space Administration (NASA), ESA, JAXA, Canadian Space Agency (CSA), German Aerospace Center (DLR) and the China National Space Administration
Positive results from these investigations combined with more frequent access to the unique microgravity environment should attract a large group of users from academia and industry
Summary
Over the past 20 years a variety of technological advances in X-ray crystallography have shortened the time required to determine the structures of large macromolecules (i.e., proteins and nucleic acids) from several years to several weeks or days. One of the remaining challenges is the ability to produce diffraction-quality crystals suitable for a detailed structural analysis. The development of automated crystallization systems combined with protein engineering (site-directed mutagenesis to enhance protein solubility and crystallization) have improved crystallization success rates, there remain hundreds of proteins that either cannot be crystallized or yield crystals of insufficient quality to support X-ray structure determination. In an attempt to address this bottleneck, an international group of scientists has explored use of a microgravity environment to crystallize macromolecules. Npj Microgravity (2015) 1, 15010; doi:10.1038/npjmgrav.2015.10; published online 3 September 2015
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