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 11
Ligand-binding sites of the structures obtained from on-chip ligand-soaking experiments using our crystallization chambers and Roadrunner I chips. (a) An aspartate molecule (pink) in complex with a sodium ion (purple sphere) is bound to the active site of thermolysin. It is involved in the fivefold coordination of the catalytic zinc ion (gray sphere) with both its amino and carboxy moieties. The 2mF_o − DF_c electron-density map at 1σ is shown as a blue mesh and catalytically important thermolysin residues (green) are labeled. (b) The 2mF_o − DF_c electron-density map at 1.5σ clearly indicates the presence of Mg²⁺-ADP (yellow sphere and pink sticks) at the active site of DRAK2.

IUCrJ

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

ISSN: 2052-2525

https://doi.org/10.1107/S2052252519007395

BIOLOGY | MEDICINE

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