On-chip crystallization for serial crystallography experiments and on-chip ligand-binding studies

Lieske, J.; Cerv, M.; Kreida, S.; Komadina, D.; Fischer, J.; Barthelmess, M.; Fischer, P.; Pakendorf, T.; Yefanov, O.; Mariani, V.; Seine, T.; Ross, B.H.; Crosas, E.; Lorbeer, O.; Burkhardt, A.; Lane, T.J.; Guenther, S.; Bergtholdt, J.; Schoen, S.; Törnroth-Horsefield, S.; Chapman, H.N.; Meents, A.

doi:10.1107/S2052252519007395

Figure 7
Exemplary 2mF_o − DF_c electron densities at 1.5σ for the structures of proteinase K (a) and thermolysin (b) derived from crystals grown on Roadrunner I chips. The Ca²⁺-binding site of proteinase K and the active site of thermolysin with two bound Zn²⁺ ions (gray spheres) are shown. Residues that are involved in ion binding and/or are functionally important are represented as sticks and labeled. For a more detailed discussion on the thermolysin structure, please see the supporting information.

IUCrJ

Volume 6| Part 4| July 2019| Pages 714-728

ISSN: 2052-2525

https://doi.org/10.1107/S2052252519007395

BIOLOGY | MEDICINE

Open

access

Follow IUCrJ

Search IUCr Journals		doi		Advanced search
Author		volume	page