Structure of radical S-adenosylmethionine methyltransferase, TsrM, from Kitasatospora setae with tryptophan substrate and SAM analog (aza-SAM) bound

Structural basis for non-radical catalysis by TsrM, a radical SAM methylase.

Tryptophan-C2-methyltransferase containing B12-binding domain

0.1 M tri-sodium citrate, pH 5.6, 20% (v/v) isopropanol, 20% (w/v) PEG 4000, and 0.05 M nickel (II) dichloride hexahydrate

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Radical SAM, Cobalamin, FeS cluster, methyltransferase, TRANSFERASE

(chain A and (resid 2 through 165 or resid 180 through 360 or resid 362 through 517 or resid 525 through 563))

(chain B and (resid 2 through 360 or resid 362 through 483 or resid 495 through 517 or resid 525 through 563))