1UVP

Structure Of The Complex Of Porcine Pancreatic Elastase In Complex With Cadmium Refined At 1.85 A Resolution (Crystal B)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.166 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

On the Influence of the Incident Photon Energy on the Radiation Damage in Crystalline Biological Samples

Weiss, M.S.Panjikar, S.Mueller-Dieckmann, C.Tucker, P.A.

(2005) J Synchrotron Radiat 12: 304

  • DOI: https://doi.org/10.1107/S0909049505003328
  • Primary Citation of Related Structures:  
    1UVO, 1UVP

  • PubMed Abstract: 

    Two series of complete and highly redundant data sets were collected at wavelengths of 1.00 and 2.00 Angstroms on a cadmium derivative of porcine pancreatic elastase (PPE). Radiation damage to the sample was evaluated qualitatively by inspecting consecutive difference electron density maps during the course of the experiment. The nature of the radiation damage was found to be identical at both wavelengths and was localized primarily at the four disulfide bridges of PPE, the cadmium site and the two methionine residues. For a quantitative examination of the radiation damage, the decrease in the peak height of the cadmium ion in various electron density maps was exploited. Again, no significant difference in radiation damage between the two wavelengths was observed. This can be rationalized by considering the wavelength dependencies of the number of diffracted photons versus the number of absorbed photons and the energy deposited in the crystal by the latter.


  • Organizational Affiliation

    EMBL Hamburg Outstation, Germany. msweiss@embl-hamburg.de


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ELASTASE 1240Sus scrofaMutation(s): 0 
EC: 3.4.21.36
UniProt
Find proteins for P00772 (Sus scrofa)
Explore P00772 
Go to UniProtKB:  P00772
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00772
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.166 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 49.75α = 90
b = 57.42β = 90
c = 74.03γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
TRUNCATEdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-10
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description