Abstract
Traditional X-ray crystallography measures the intensities of photons scattered into sharp Bragg peaks, yielding the average structure for a protein in the crystalline state. Diffuse X-ray scattering measures the non-Bragg signal which is spread throughout the (reciprocal) space between Bragg reflections. This diffuse scattering signal encodes the fluctuations in the protein crystal structure due to atomic and molecular disorder. In this study we analyze the X-ray diffuse scattering from a protein binding protein (from Bacillus halodurans, 3K9I). The data can be accounted for using a simple Markov model for the crystal disorder. This model allows for determination of the correlation coefficients for displacements between nearest neighbor protein molecules in the crystal lattice.
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.
