8PX0

Structure of ribonuclease A, solved at wavelength 2.75 A


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.

El 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.

(2023) Commun Chem 6: 219-219

  • DOI: https://doi.org/10.1038/s42004-023-01014-0
  • Primary Citation of Related Structures:  
    8PWN, 8PX0, 8PX1, 8PX4, 8PX5, 8PX7, 8PX9, 8PXC, 8PXG, 8PXH, 8PXJ, 8PXK, 8PXL, 8PYV, 8PYZ, 8PZ4, 8PZ5

  • 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.


  • Organizational Affiliation

    Diamond Light Source, Harwell Science and Innovation Campus, -, OX110DE, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ribonuclease pancreatic
A, B
124Bos taurusMutation(s): 0 
Gene Names: RNASE1RNS1
EC: 4.6.1.18
UniProt
Find proteins for P61823 (Bos taurus)
Explore P61823 
Go to UniProtKB:  P61823
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP61823
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
0U
Query on 0U

Download Ideal Coordinates CCD File 
C [auth A]L-URIDINE-5'-MONOPHOSPHATE
C9 H13 N2 O9 P
DJJCXFVJDGTHFX-PSQAKQOGSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.201 
  • R-Value Observed: 0.203 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.98α = 90
b = 32.62β = 90.16
c = 72.49γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
HKL2Mapphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Diamond Light SourceUnited Kingdom--

Revision History  (Full details and data files)

  • Version 1.0: 2023-10-25
    Type: Initial release
  • Version 1.1: 2024-11-06
    Changes: Structure summary