Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6

Ahlqvist, J.; Linares-Pastén, J.A.; Håkansson, M.; Jasilionis, A.; Kwiatkowska-Semrau, K.; Friðjónsson, Ó.H.; Kaczorowska, A.-K.; Dabrowski, S.; Ævarsson, A.; Hreggviðsson, G.Ó.; Al-Karadaghi, S.; Kaczorowski, T.; Nordberg Karlsson, E.

doi:10.1107/S2059798321012298

Figure 1
(a) Lanes 1 and 2: SDS–PAGE of crude extract supernatant and purified Hjc_15-6 protein produced in shake flasks using complex (LB) medium. Lanes 3 and 4 correspond to lanes 1 and 2 where the crude extract supernatant and purified Hjc_15-6 protein were instead produced in a fermenter using defined (mAT) medium. Lanes L contain molecular-mass markers (Bio-Rad). (b) Internally calibrated mass spectrogram (z = +1) of recombinant Hjc_15-6 protein overproduced in shake flasks using complex (LB) medium (upper black spectrogram) and Hjc_15-6 protein overproduced in a fermenter using defined (mAT) medium (lower pink spectrogram). (c) Externally calibrated mass spectrogram (z = +2) of overproduced Hjc_15-6 protein. The lower blue spectrogram (graph A) corresponds to Hjc_15-6 that was overproduced in shake flasks using complex (LB) medium and the upper green spectogram (graph B) corresponds to Hjc_15-6 protein that was overproduced in a fermenter using defined (mAT) medium. Peaks A2 and B2 have an additional mass of 96.4 and 97.3 Da compared with peaks A1 and B1, respectively, and peaks B3 and B4 have an additional mass of 97.6 and 93.2 Da compared with peaks B2 and B3, respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 2| February 2022| Pages 212-227

https://doi.org/10.1107/S2059798321012298

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