TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production， morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report， N-terminally His-tagged recombinant TylP protein (rTylP) was overproduced in Escherichia coli and purified to homogeneity. The rTylP protein was crystallized from a reservoir solution comprising 34%(v/v) ethylene glycol and 5%(v/v) glycerol. The protein crystals diffracted X-rays to 3.05?? resolution and belonged to the trigonal space group P321， with unit-cell parameters a = b = 126.62， c = 95.63??.
TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production， morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report， N-terminally His-tagged recombinant TylP protein (rTylP) was overproduced in Escherichia coli and purified to homogeneity. The rTylP protein was crystallized from a reservoir solution comprising 34%(v/v) ethylene glycol and 5%(v/v) glycerol. The protein crystals diffracted X-rays to 3.05?? resolution and belonged to the trigonal space group P321， with unit-cell parameters a = b = 126.62， c = 95.63??.
