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8AR6

Structure of Delta 57-NCOA7 in space group P41212

Summary for 8AR6
Entry DOI10.2210/pdb8ar6/pdb
DescriptorNuclear receptor coactivator 7 (2 entities in total)
Functional Keywordshuman ncoa7, viral restriction factors, antiviral protein
Biological sourceHomo sapiens (human)
Total number of polymer chains3
Total formula weight62442.87
Authors
Campeotto, I.,Foster, T. (deposition date: 2022-08-15, release date: 2023-05-24, 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 (2.2 Å)
Structure validation

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数据于2025-12-17公开中

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