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Crystallization and X‐ray crystallographic analysis of recombinant TylP, a putative γ‐butyrolactone receptor protein from Streptomyces fradiae
Author(s) -
Mohd-Sharif Nurhikmah,
Shaibullah Sofiyah,
Givajothi Vasanthakumar,
Tan Cheng-Seng,
Ho Kok Lian,
Teh Aik-Hong,
Baharum Syarul Nataqain,
Waterman Jitka,
Ng Chyan Leong
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17001212
Subject(s) - streptomyces fradiae , tylosin , recombinant dna , ethylene glycol , escherichia coli , crystallization , glycerol , biology , crystallography , streptomyces , chemistry , stereochemistry , biochemistry , gene , antibiotics , bacteria , actinomycetales , organic chemistry , genetics
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 P 3 1 21, with unit‐cell parameters a = b = 126.62, c = 95.63 Å.