5NJM

Lysozyme room-temperature structure determined by serial millisecond crystallography

Summary for 5NJM

• Entry DOI: 10.2210/pdb5njm/pdb
• Descriptor: Lysozyme C (2 entities in total)
• Functional Keywords: room-temperature, serial crystallography, hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Weinert, T.,Vera, L.,Marsh, M.,James, D.,Gashi, D.,Nogly, P.,Jaeger, K.,Standfuss, J. (deposition date: 2017-03-29, release date: 2017-09-27, Last modification date: 2024-11-13)

Primary citation

Weinert, T.,Olieric, N.,Cheng, R.,Brunle, S.,James, D.,Ozerov, D.,Gashi, D.,Vera, L.,Marsh, M.,Jaeger, K.,Dworkowski, F.,Panepucci, E.,Basu, S.,Skopintsev, P.,Dore, A.S.,Geng, T.,Cooke, R.M.,Liang, M.,Prota, A.E.,Panneels, V.,Nogly, P.,Ermler, U.,Schertler, G.,Hennig, M.,Steinmetz, M.O.,Wang, M.,Standfuss, J.
Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.
Nat Commun, 8:542-542, 2017

PubMed Abstract: Historically, room-temperature structure determination was succeeded by cryo-crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond crystallography at a synchrotron beamline equipped with high-viscosity injector and high frame-rate detector allows typical crystallographic experiments to be performed at room-temperature. Using a crystal scanning approach, we determine the high-resolution structure of the radiation sensitive molybdenum storage protein, demonstrate soaking of the drug colchicine into tubulin and native sulfur phasing of the human G protein-coupled adenosine receptor. Serial crystallographic data for molecular replacement already converges in 1,000-10,000 diffraction patterns, which we collected in 3 to maximally 82 minutes. Compared with serial data we collected at a free-electron laser, the synchrotron data are of slightly lower resolution, however fewer diffraction patterns are needed for de novo phasing. Overall, the data we collected by room-temperature serial crystallography are of comparable quality to cryo-crystallographic data and can be routinely collected at synchrotrons.Serial crystallography was developed for protein crystal data collection with X-ray free-electron lasers. Here the authors present several examples which show that serial crystallography using high-viscosity injectors can also be routinely employed for room-temperature data collection at synchrotrons.

PubMed: 28912485
DOI: 10.1038/s41467-017-00630-4

Experimental method

X-RAY DIFFRACTION (1.5 Å)