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.
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