Citation
Mohd Sharif, Nurhikmah and Shaibullah, Sofiyah and Givajothi, Vasanthakumar and Tan, Cheng Seng and Ho, Kok Lian and Teh, Aik Hong and Baharum, Syarul Nataqain and Waterman, Jitka and Ng, Chyan Leong
(2017)
Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae.
Acta Crystallographica Section F: Structural Biology Communications, 73 (2).
pp. 109-115.
ISSN 2053-230X
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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Official URL or Download Paper: http://onlinelibrary.wiley.com/doi/10.1107/S205323...
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Additional Metadata
| Item Type: | Article |
|---|---|
| Divisions: | Faculty of Medicine and Health Science |
| DOI Number: | https://doi.org/10.1107/S2053230X17001212 |
| Publisher: | International Union of Crystallography |
| Keywords: | Streptomyces fradiae; Recombinant TylP protein; γ-butyrolactone; GBL; Transcription factors; Tylosin |
| Depositing User: | Nabilah Mustapa |
| Date Deposited: | 14 Mar 2018 03:01 |
| Last Modified: | 14 Mar 2018 03:01 |
| Altmetrics: | http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1107/S2053230X17001212 |
| URI: | http://psasir.upm.edu.my/id/eprint/59627 |
| Statistic Details: | View Download Statistic |
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