Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive

Zielinski, K.A.; Prester, A.; Andaleeb, H.; Bui, S.; Yefanov, O.; Catapano, L.; Henkel, A.; Wiedorn, M.O.; Lorbeer, O.; Crosas, E.; Meyer, J.; Mariani, V.; Domaracky, M.; White, T.A.; Fleckenstein, H.; Sarrou, I.; Werner, N.; Betzel, C.; Rohde, H.; Aepfelbacher, M.; Chapman, H.N.; Perbandt, M.; Steiner, R.A.; Oberthuer, D.

doi:10.1107/S2052252522010193

Figure 7
Comparison of the overall structures of NhGH11 xylanase obtained by cryoMX (cyan) and RT-SSX (magenta, 40 000-image dataset). (a) All-atom `stick' depiction of the proteins, allowing us to assess the alignment of the sidechains. (b) Cartoon-plot for better visibility of the overall fold and and residues E89 and E180 that form the catalytic center. These residues overlap almost perfectly for both datasets.

IUCrJ

Volume 9| Part 6| November 2022| Pages 778-791

ISSN: 2052-2525

https://doi.org/10.1107/S2052252522010193

PHYSICS | FELS

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