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 significa...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2000-06, Vol.56 (6), p.785-788
Main Authors: Sharff, Andrew J., Koronakis, Eva, Luisi, Ben, Koronakis, Vassillis
Format: Article
Language:English
Subjects:
Amino Acid Substitution - genetics
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - genetics
Crystallization
Crystallography, X-Ray - methods
Escherichia coli
Escherichia coli Proteins
Hydrogen Peroxide - chemistry
MAD
Membrane Transport Proteins
Mercaptoethanol - chemistry
Oxidation-Reduction
Recombinant Proteins - chemistry
Reducing Agents - chemistry
Selenomethionine - chemistry
selenomethionine proteins
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Summary: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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S090744490000370X