5DM9

XFEL structure of hen egg-white lysozyme solved using a droplet injector at SACLA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.211 
  • R-Value Work: 0.182 
  • R-Value Observed: 0.184 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Microcrystal delivery by pulsed liquid droplet for serial femtosecond crystallography.

Mafune, F.Miyajima, K.Tono, K.Takeda, Y.Kohno, J.Y.Miyauchi, N.Kobayashi, J.Joti, Y.Nango, E.Iwata, S.Yabashi, M.

(2016) Acta Crystallogr D Struct Biol 72: 520-523

  • DOI: https://doi.org/10.1107/S2059798316001480
  • Primary Citation of Related Structures:  
    5DM9

  • PubMed Abstract: 

    A liquid-droplet injector has been developed that delivers pristine microcrystals to an X-ray irradiation area for conducting serial femtosecond crystallography (SFX) with an X-ray free-electron laser (XFEL). By finely tuning the pulsed liquid droplets in time and space, a high hit rate of the XFEL pulses to microcrystals in the droplets was achieved for measurements using 5 µm tetragonal lysozyme crystals, which produced 4265 indexable diffraction images in about 30 min. The structure was determined at a resolution of 2.3 Å from <0.3 mg of protein. With further improvements such as reduction of the droplet size, liquid droplets have considerable potential as a crystal carrier for SFX with low sample consumption.


  • Organizational Affiliation

    Department of Basic Science, School of Arts and Sciences, The University of Tokyo, Komaba, Meguro, Tokyo 153-8902, Japan.


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
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.2α = 90
b = 79.2β = 90
c = 38γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
Cootmodel building
REFMACphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-04-13
    Type: Initial release
  • Version 1.1: 2018-01-24
    Changes: Data collection, Derived calculations
  • Version 1.2: 2018-03-14
    Changes: Database references
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references
  • Version 1.4: 2023-11-08
    Changes: Refinement description
  • Version 1.5: 2024-10-16
    Changes: Structure summary