Can anomalous signal of sulfur become a tool for solving protein crystal structures?
A general method for solving the phase problem from native crystals of macromolecules has long eluded structural biology. For well diffracting crystals this goal can now be achieved, as is shown here, thanks to modern data collection techniques and new statistical phasing algorithms. Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.
Dauter
Z
Z
National Cancer Institute, Frederick and Brookhaven National Laboratory, Building 725A-X9, Upton, NY, 11973, USA. dauter@bnl.gov
Dauter
M
M
de La Fortelle
E
E
Bricogne
G
G
Sheldrick
G M
GM
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002713:Chlorine / Q000032:analysis; D003196:Computer Graphics; D018360:Crystallography, X-Ray / Q000379:methods*; D005583:Fourier Analysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D013455:Sulfur / Q000737:chemistry*
D002713:Chlorine; D013455:Sulfur; D009113:Muramidase