4ETA

Lysozyme, room temperature, 400 kGy dose


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.180 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

High-resolution protein structure determination by serial femtosecond crystallography.

Boutet, S.Lomb, L.Williams, G.J.Barends, T.R.Aquila, A.Doak, R.B.Weierstall, U.DePonte, D.P.Steinbrener, J.Shoeman, R.L.Messerschmidt, M.Barty, A.White, T.A.Kassemeyer, S.Kirian, R.A.Seibert, M.M.Montanez, P.A.Kenney, C.Herbst, R.Hart, P.Pines, J.Haller, G.Gruner, S.M.Philipp, H.T.Tate, M.W.Hromalik, M.Koerner, L.J.van Bakel, N.Morse, J.Ghonsalves, W.Arnlund, D.Bogan, M.J.Caleman, C.Fromme, R.Hampton, C.Y.Hunter, M.S.Johansson, L.C.Katona, G.Kupitz, C.Liang, M.Martin, A.V.Nass, K.Redecke, L.Stellato, F.Timneanu, N.Wang, D.Zatsepin, N.A.Schafer, D.Defever, J.Neutze, R.Fromme, P.Spence, J.C.Chapman, H.N.Schlichting, I.

(2012) Science 337: 362-364

  • DOI: https://doi.org/10.1126/science.1217737
  • Primary Citation of Related Structures:  
    4ET8, 4ET9, 4ETA, 4ETB, 4ETC, 4ETD, 4ETE

  • PubMed Abstract: 

    Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.


  • Organizational Affiliation

    Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lysozyme C129Gallus gallusMutation(s): 0 
EC: 3.2.1.17
UniProt
Find proteins for P00698 (Gallus gallus)
Explore P00698 
Go to UniProtKB:  P00698
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00698
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CL
Query on CL

Download Ideal Coordinates CCD File 
B [auth A]CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.91 Å
  • R-Value Free: 0.180 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.161 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.3α = 90
b = 79.3β = 90
c = 38.2γ = 90
Software Package:
Software NamePurpose
PHENIXmodel building
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2012-06-13
    Type: Initial release
  • Version 1.1: 2012-08-08
    Changes: Database references
  • Version 1.2: 2017-11-15
    Changes: Refinement description
  • Version 1.3: 2024-11-06
    Changes: Data collection, Database references, Derived calculations, Structure summary