Title :
Analysis of Simultaneous Multiwavelength Anomalous Diffraction for phasing protein crystals
Author :
Engel, Matthew A. ; Allaire, Marc
Author_Institution :
State Univ. of New York-Stony Brook, Stony Brook
Abstract :
Macromolecular crystallography is a burgeoning field bridging the disciplines of biological chemistry, physics and material science. The diffraction of protein crystals is frequently required by pharmaceutical companies during the drug development process. Both intensity and phase of diffracted x-rays are required to solve a new crystal structure. Phases can be determined using the multiwavelength anomalous diffraction method (MAD). Simultaneous MAD (SMAD) has been proposed to significantly reduce the length of synchrotron data collection leading to faster structure determination. Analysis of MAD images collected at the peak and edge wavelengths reveal overlapping HKL reflections.
Keywords :
X-ray diffraction; crystal structure; drugs; macromolecules; molecular biophysics; proteins; synchrotron radiation; MAD image analysis; X-ray intensity; biological chemistry; crystal structure; diffracted X-ray phase; drug development process; macromolecular crystallography; multiwavelength anomalous diffraction method; pharmaceutical companies; protein crystals; synchrotron data collection; Biology; Chemistry; Crystallography; Crystals; Drugs; Materials science and technology; Pharmaceuticals; Physics; Protein engineering; X-ray diffraction;
Conference_Titel :
Bioengineering Conference, 2007. NEBC '07. IEEE 33rd Annual Northeast
Conference_Location :
Long Island, NY
Print_ISBN :
978-1-4244-1033-0
Electronic_ISBN :
978-1-4244-1033-0
DOI :
10.1109/NEBC.2007.4413321
