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UV absorption spectra of purified IscS enzymes from G. stearothermophilus V. Protein solutions (1.5 mg/ml) of wild-type IscS (A) and mutant IscS/K213A (B) were prepared in 10 mM Tris-HCl (pH 8.0)-5% glycerol and scanned using an HP Agilent 8453 spectrophotometer. Wild-type IscS has an absorption maximum at 421 nm characteristic of many PLP-dependent enzymes.
