7ZCK
Room temperature crystal structure of PhnD from Synechococcus MITS9220 in complex with phosphate
Summary for 7ZCK
Entry DOI | 10.2210/pdb7zck/pdb |
Descriptor | Phosphonate ABC type transporter/ substrate binding component, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | substrate-binding protein, marine cyanobacteria, urea-binding protein, transport protein |
Biological source | Synechococcus sp. MIT S9220 |
Total number of polymer chains | 1 |
Total formula weight | 30567.31 |
Authors | Mikolajek, H.,Shah, B.S.,Paulsen, I.T.,Sandy, J.,Sanchez-Weatherby, J. (deposition date: 2022-03-28, release date: 2022-05-04, Last modification date: 2024-02-07) |
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 Cited by 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: 37199504DOI: 10.1107/S2052252523003810 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report