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Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Feb2017, Vol. 73 Issue 2, p109-115, 6p
- Publication Year :
- 2017
-
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 P3<subscript>1</subscript>21, with unit-cell parameters a = b = 126.62, c = 95.63 Å. [ABSTRACT FROM AUTHOR]
- Subjects :
- STREPTOMYCES fradiae
BACTERIAL protein crystallography
BUTYROLACTONES
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 73
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 121184904
- Full Text :
- https://doi.org/10.1107/S2053230X17001212