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Tellurite Resistance Transformation for Simplified X‐Ray Crystallographic Protein Structure Analysis
Author(s) -
Mancuso Matthew Cian,
Boles Jeffrey O
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.670.7
Subject(s) - selenium , tellurium , crystallography , methionine , x ray , resolution (logic) , x ray crystallography , protein crystallization , chemistry , transformation (genetics) , diffraction , amino acid , materials science , gene , optics , biochemistry , crystallization , physics , inorganic chemistry , computer science , organic chemistry , artificial intelligence
One of the most common techniques for determining protein structure is X‐ray crystallography using selenium‐substituted amino acids. The disadvantage of this method, is the high cost and long wait times for a synchrotron x‐ray source, the only device capable of MAD (Multi‐wavelength Anomalous Diffraction), which is necessary for resolution of a structure with selenium. Telluromethionine‐containing proteins, on the other hand, can be imaged using more common x‐ray crystallographic devices. In previous work, tellurium has shown to be toxic to bacterial cells which causes poor integration and low cell growth rates. This is being overcome via the introduction of a tellurium resistance gene into a methionine auxotroph to mitigate toxicity.