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8PX0

Structure of ribonuclease A, solved at wavelength 2.75 A

Summary for 8PX0
Entry DOI10.2210/pdb8px0/pdb
DescriptorRibonuclease pancreatic, L-URIDINE-5'-MONOPHOSPHATE (3 entities in total)
Functional Keywordsrnase a, membrane protein
Biological sourceBos taurus (cattle)
Total number of polymer chains2
Total formula weight27740.83
Authors
El Omari, K.,Duman, R.,Mykhaylyk, V.,Orr, C.,Romano, M.,Beis, K.,Wagner, A. (deposition date: 2023-07-22, release date: 2023-10-25, Last modification date: 2024-11-06)
Primary citationEl Omari, K.,Duman, R.,Mykhaylyk, V.,Orr, C.M.,Latimer-Smith, M.,Winter, G.,Grama, V.,Qu, F.,Bountra, K.,Kwong, H.S.,Romano, M.,Reis, R.I.,Vogeley, L.,Vecchia, L.,Owen, C.D.,Wittmann, S.,Renner, M.,Senda, M.,Matsugaki, N.,Kawano, Y.,Bowden, T.A.,Moraes, I.,Grimes, J.M.,Mancini, E.J.,Walsh, M.A.,Guzzo, C.R.,Owens, R.J.,Jones, E.Y.,Brown, D.G.,Stuart, D.I.,Beis, K.,Wagner, A.
Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.
Commun Chem, 6:219-219, 2023
Cited by
PubMed Abstract: Despite recent advances in cryo-electron microscopy and artificial intelligence-based model predictions, a significant fraction of structure determinations by macromolecular crystallography still requires experimental phasing, usually by means of single-wavelength anomalous diffraction (SAD) techniques. Most synchrotron beamlines provide highly brilliant beams of X-rays of between 0.7 and 2 Å wavelength. Use of longer wavelengths to access the absorption edges of biologically important lighter atoms such as calcium, potassium, chlorine, sulfur and phosphorus for native-SAD phasing is attractive but technically highly challenging. The long-wavelength beamline I23 at Diamond Light Source overcomes these limitations and extends the accessible wavelength range to λ = 5.9 Å. Here we report 22 macromolecular structures solved in this extended wavelength range, using anomalous scattering from a range of elements which demonstrate the routine feasibility of lighter atom phasing. We suggest that, in light of its advantages, long-wavelength crystallography is a compelling option for experimental phasing.
PubMed: 37828292
DOI: 10.1038/s42004-023-01014-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2024-11-06公开中

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