Abstract
A CONSIDERABLE problem hampering the analysis of protein crystal structures has been the damage caused to the crystals by the X-ray beam. Another limiting factor has been the resolution in the diffraction pattern. To increase the useful life of a protein crystal in the X-ray beam1, single crystal monochromators and low temperatures have been used. We now report that styrene and other vinyl monomers can decrease the radiation damage of the crystal in the X-ray beam by a factor of as much as 10, and extend the diffraction pattern so that higher angle reflections can be measured.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
