Oxidation of selenomethionine: some MADness in the method!
Since it was first reported, the multiwavelength anomalous diffraction (MAD) technique for the determination of protein structures has become widely accepted and increasingly popular. Here, it is demonstrated that the anomalous signal from selenomethione (SeMet) substituted proteins can be significantly enhanced by oxidation.
Sharff
A J
AJ
Department of Biochemistry, University of Cambridge, England. andrew@cryst.bioc.cam.ac.uk
Koronakis
E
E
Luisi
B
B
Koronakis
V
V
D019943:Amino Acid Substitution / Q000235:genetics; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D006861:Hydrogen Peroxide / Q000737:chemistry; D026901:Membrane Transport Proteins; D008623:Mercaptoethanol / Q000737:chemistry; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry; D019163:Reducing Agents / Q000737:chemistry; D012645:Selenomethionine / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; D019163:Reducing Agents; C073126:tolC protein, E coli; D008623:Mercaptoethanol; D012645:Selenomethionine; D006861:Hydrogen Peroxide