Abstract
Correction for ‘Structure of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 reveals a novel fold of the flexible loop’ by Yanhui Liu et al., RSC Adv., 2016, 6, 41743–41750.
Highlights
Correction: Structure of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 reveals a novel fold of the flexible loop
Correction for ‘Structure of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 reveals a novel fold of the flexible loop’ by Yanhui Liu et al, RSC Adv., 2016, 6, 41743–41750
At 60 C, the activity of EcMAT underwent a quick decrease and dropped to almost 30% of the initial activity a er 25 hours, whereas TtMAT showed even higher activity (60 C) than the initial activity during the same time (Fig. 2B)
Summary
Correction: Structure of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 reveals a novel fold of the flexible loop. Cite this: RSC Adv., 2016, 6, 44993 Correction for ‘Structure of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27 reveals a novel fold of the flexible loop’ by Yanhui Liu et al, RSC Adv., 2016, 6, 41743–41750.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
