4B0D

CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME FROM AN AUTO HARVESTED CRYSTAL


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.10 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal Direct: A New Method for Automated Crystal Harvesting Based on Laser-Induced Photoablation of Thin Films

Cipriani, F.Rower, M.Landret, C.Zander, U.Felisaz, F.Marquez, J.A.

(2012) Acta Crystallogr D Biol Crystallogr 68: 1393

  • DOI: https://doi.org/10.1107/S0907444912031459
  • Primary Citation of Related Structures:  
    4AXR, 4AXT, 4AXU, 4B0D

  • PubMed Abstract: 

    The use of automated systems for crystallization and X-ray data collection is now widespread. However, these two steps are separated by the need to transfer crystals from crystallization supports to X-ray data-collection supports, which is a difficult manual operation. Here, a new approach is proposed called CrystalDirect (CD) which enables full automation of the crystal-harvesting process. In this approach, crystals are grown on ultrathin films in a newly designed vapour-diffusion crystallization plate and are recovered by excision of the film through laser-induced photoablation. The film pieces containing crystals are then directly attached to a pin for X-ray data collection. This new method eliminates the delicate step of `crystal fishing', thereby enabling full automation of the crystal-mounting process. Additional advantages of this approach include the absence of mechanical stress and that it facilitates handling of microcrystals. The CD crystallization plates are also suitable for in situ crystal screening with minimal X-ray background. This method could enable the operational integration of highly automated crystallization and data-collection facilities, minimizing the delay between crystal identification and diffraction measurements. It can also contribute significantly to the advancement of challenging projects that require the systematic testing of large numbers of crystals.


  • Organizational Affiliation

    Grenoble Outstation, European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble, France. [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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.10 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.187 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.25α = 90
b = 78.25β = 90
c = 37.915γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-10-24
    Type: Initial release
  • Version 1.1: 2024-10-23
    Changes: Data collection, Database references, Other, Structure summary