5AMW

Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 2 protein (A141F) processed with the CrystalDirect automated mounting and cryo-cooling technology


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.223 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Automated Harvesting and Processing of Protein Crystals Through Laser Photoablation.

Zander, U.Hoffmann, G.Cornaciu, I.Marquette, J.-P.Papp, G.Landret, C.Seroul, G.Sinoir, J.Roewer, M.Felisaz, F.Rodriguez-Puente, S.Mariaule, V.Murphy, P.Mathieu, M.Cipriani, F.Marquez, J.A.

(2016) Acta Crystallogr D Biol Crystallogr 72: 454

  • DOI: https://doi.org/10.1107/S2059798316000954
  • Primary Citation of Related Structures:  
    5AMW, 5AMX, 5AMZ, 5AN4, 5AND, 5ANE, 5ANG, 5ANI, 5ANJ, 5ANK, 5ANL, 5ANO, 5DWP, 5EBH

  • PubMed Abstract: 

    Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.


  • Organizational Affiliation

    Grenoble Outstation, European Molecular Biology Laboratory; Unit of Virus Host-Cell Interactions (UMI 3265), University Grenoble Alpes-EMBL-CNRS, 71 Avenue des Martyrs, 38042 Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fra a 2 allergen
A, B
162Fragaria x ananassaMutation(s): 0 
Gene Names: Fraa2
UniProt
Find proteins for D0E0C6 (Fragaria ananassa)
Explore D0E0C6 
Go to UniProtKB:  D0E0C6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD0E0C6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.223 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 105.559α = 90
b = 41.463β = 116.28
c = 92.058γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-04-13
    Type: Initial release
  • Version 1.1: 2016-04-20
    Changes: Data collection, Database references
  • Version 1.2: 2016-05-11
    Changes: Data collection
  • Version 1.3: 2018-12-05
    Changes: Data collection, Database references, Source and taxonomy, Structure summary