8A9D

Multicrystal room temperature structure of Lysozyme collected using a double multilayer monochromator.

Summary for 8A9D

• Entry DOI: 10.2210/pdb8a9d/pdb
• Descriptor: Lysozyme, SODIUM ION (3 entities in total)
• Functional Keywords: lysozyme, multi-crystal, dmm, multilayer mmonochromator, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 14354.15

Authors

Sandy, J.,Cheruvara, H.,Mikolajek, H.,Sanchez-Weatherby, J. (deposition date: 2022-06-28, release date: 2022-07-20, Last modification date: 2024-11-06)

Primary citation

Mikolajek, H.,Sanchez-Weatherby, J.,Sandy, J.,Gildea, R.J.,Campeotto, I.,Cheruvara, H.,Clarke, J.D.,Foster, T.,Fujii, S.,Paulsen, I.T.,Shah, B.S.,Hough, M.A.
Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi.
Iucrj, 10:420-429, 2023

PubMed Abstract: The utility of X-ray crystal structures determined under ambient-temperature conditions is becoming increasingly recognized. Such experiments can allow protein dynamics to be characterized and are particularly well suited to challenging protein targets that may form fragile crystals that are difficult to cryo-cool. Room-temperature data collection also enables time-resolved experiments. In contrast to the high-throughput highly automated pipelines for determination of structures at cryogenic temperatures widely available at synchrotron beamlines, room-temperature methodology is less mature. Here, the current status of the fully automated ambient-temperature beamline VMXi at Diamond Light Source is described, and a highly efficient pipeline from protein sample to final multi-crystal data analysis and structure determination is shown. The capability of the pipeline is illustrated using a range of user case studies representing different challenges, and from high and lower symmetry space groups and varied crystal sizes. It is also demonstrated that very rapid structure determination from crystals in situ within crystallization plates is now routine with minimal user intervention.

PubMed: 37199504
DOI: 10.1107/S2052252523003810

Experimental method

X-RAY DIFFRACTION (2.1 Å)