6CLL

1.02 A MicroED structure of GSNQNNF at 1.2 e- / A^2


Experimental Data Snapshot

  • Method: ELECTRON CRYSTALLOGRAPHY
  • Resolution: 1.02 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.249 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.

Hattne, J.Shi, D.Glynn, C.Zee, C.T.Gallagher-Jones, M.Martynowycz, M.W.Rodriguez, J.A.Gonen, T.

(2018) Structure 26: 759-766.e4

  • DOI: https://doi.org/10.1016/j.str.2018.03.021
  • Primary Citation of Related Structures:  
    6CL7, 6CL8, 6CL9, 6CLA, 6CLB, 6CLC, 6CLD, 6CLE, 6CLF, 6CLG, 6CLH, 6CLI, 6CLJ, 6CLK, 6CLL, 6CLM, 6CLN, 6CLO, 6CLP, 6CLQ, 6CLR, 6CLS, 6CLT

  • PubMed Abstract: 

    Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data.


  • Organizational Affiliation

    Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles CA 90095, USA; Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA 20147, USA.


Macromolecules

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GSNQNNF7synthetic constructMutation(s): 0 
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON CRYSTALLOGRAPHY
  • Resolution: 1.02 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.249 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 4.84α = 83.8
b = 14.09β = 85.34
c = 17.38γ = 82.94
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTREFMAC5.8.0194

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-05-16
    Type: Initial release
  • Version 1.1: 2024-03-13
    Changes: Data collection, Database references, Derived calculations