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 8
Detailed view of the alignment of all residues composing the active site of NhGH11 xylanase. The cryoMX residues are shown in cyan, the full 40 000-image dataset structure are shown in magenta and additionally the active site residues from the structure obtained by refinement against the 1000-image dataset are shown in purple. The strongest deviations from the cryoMX reference can be observed in Arg125, all other residues overlap almost perfectly.

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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