Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ -butyrolactone receptor protein from Streptomyces fradiae

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   Å resolution and belonged to the trigonal space group P3121, with unit-cell parameters a = b = 126.62, c = 95.63   Å .

Source: Acta Crystallographica Section F - January 30, 2017 Category: Biochemistry Authors: Mohd-Sharif, N. Shaibullah, S. Givajothi, V. Tan, C.-S. Ho, K.L. Teh, A.-H. Baharum, S.N. Waterman, J. Ng, C.L. Tags: Streptomyces fradiae recombinant TylP protein γ -butyrolactone GBL transcription factors tylosin research communications Source Type: research