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.
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