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

fYear

2007

fDate

10-11 March 2007

Firstpage

146

Lastpage

147

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;

fLanguage

English

Publisher

ieee

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

Type

conf

DOI

10.1109/NEBC.2007.4413321

Filename

4413321