Title |
Crystallization and X‐ray crystallographic analysis of recombinant TylP, a putative γ‐butyrolactone receptor protein from Streptomyces fradiae
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Published in |
Acta Crystallographica Section F: Structural Biology Communications, January 2017
|
DOI | 10.1107/s2053230x17001212 |
Pubmed ID | |
Authors |
Nurhikmah Mohd-Sharif, Sofiyah Shaibullah, Vasanthakumar Givajothi, Cheng-Seng Tan, Kok Lian Ho, Aik-Hong Teh, Syarul Nataqain Baharum, Jitka Waterman, Chyan Leong Ng |
Abstract |
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 Å resolution and belonged to the trigonal space group P3121, with unit-cell parameters a = b = 126.62, c = 95.63 Å. |
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