The multiwavelength anomalous dispersion (MAD) method of protein structure
determination is becoming a routine technique in protein crystallography, T
he increased number of wavelength-tuneable synchrotron beamlines capable of
performing challenging MAD experiments, coupled with the widespread availa
bility of charge-coupled device (CCD) based X-ray detectors with fast read-
out times have brought MAD structure determination to a new exciting level.
Ultrafast MAD data collection is now possible and, with the widespread use
of selenium in the form of selenomethionine for phase determination, the m
ethod is growing in popularity. Recent developments in crystallographic sof
tware are complementing the above advances, paving the way for rapid protei
n structure determination. An overview of a typical MAD experiment is descr
ibed, with emphasis on the rates and quality of data acquisition now achiev
able at third-generation synchrotron sources.