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7ZCK

Room temperature crystal structure of PhnD from Synechococcus MITS9220 in complex with phosphate

Summary for 7ZCK
Entry DOI10.2210/pdb7zck/pdb
DescriptorPhosphonate ABC type transporter/ substrate binding component, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordssubstrate-binding protein, marine cyanobacteria, urea-binding protein, transport protein
Biological sourceSynechococcus sp. MIT S9220
Total number of polymer chains1
Total formula weight30567.31
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 citationMikolajek, 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: 37199504
DOI: 10.1107/S2052252523003810
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

226707

건을2024-10-30부터공개중

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