3UBC

Oxygen-bound hell's gate globin I by LB nanotemplate method


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.208 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Oxygen-bound Hell's gate globin I by classical versus LB nanotemplate method.

Pechkova, E.Scudieri, D.Belmonte, L.Nicolini, C.

(2012) J Cell Biochem 8: 793-794

  • DOI: https://doi.org/10.1002/jcb.24131
  • Primary Citation of Related Structures:  
    3UBC, 3UBV

  • PubMed Abstract: 

    X-ray atomic structure of recombinant Hell's gate globin I (HGbI) from Methylacidophilum infernorum was calculated from the X-ray diffraction data of two different types of crystals: obtained by classical hanging drop and by LB nanotemplate method under the same crystallization conditions. After the accurate comparison of crystallographic parameters and electron density maps of two structures they appears to be quite similar, while the quality of the crystals grown by LB nanotemplate method was higher then of those grown by classical method. Indeed, the resolution of the LB crystal structure was 1.65 Å, while classical crystals showed only 3.2 Å resolution. Moreover, the reproducibility of this result in the case of LB crystals was much better-nine crystals from 10 gave the same structural results, while only two of 10 classical crystals were appropriate for the X-ray structure resolution.


  • Organizational Affiliation

    Nanobiotechnology and Biophysics Laboratories, Department Experimental Medicine, University of Genova, Genova, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hemoglobin-like flavoproteinA,
B [auth D],
C [auth G]
131Methylacidiphilum infernorum V4Mutation(s): 0 
Gene Names: hmpMinf_1095
UniProt
Find proteins for B3DUZ7 (Methylacidiphilum infernorum (isolate V4))
Explore B3DUZ7 
Go to UniProtKB:  B3DUZ7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB3DUZ7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.208 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.227α = 90
b = 126.533β = 90
c = 148.236γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
XSCALEdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-03-28
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references, Derived calculations