6MEZ

X-ray structure of the Fenna-Matthews-Olsen antenna complex from Prosthecochloris aestuarii

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.134 

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Literature

Neutron and X-ray analysis of the Fenna-Matthews-Olson photosynthetic antenna complex from Prosthecochloris aestuarii.

Lu, X., Selvaraj, B., Ghimire-Rijal, S., Orf, G.S., Meilleur, F., Blankenship, R.E., Cuneo, M.J., Myles, D.A.A.

(2019) Acta Crystallogr F Struct Biol Commun 75: 171-175

  • DOI: https://doi.org/10.1107/S2053230X19000724
  • Primary Citation of Related Structures:  
    6MEZ

  • PubMed Abstract: 

    The Fenna-Matthews-Olson protein from Prosthecochloris aestuarii (PaFMO) has been crystallized in a new form that is amenable to high-resolution X-ray and neutron analysis. The crystals belonged to space group H3, with unit-cell parameters a = b = 83.64, c = 294.78 Å, and diffracted X-rays to ∼1.7 Å resolution at room temperature. Large PaFMO crystals grown to volumes of 0.3-0.5 mm 3 diffracted neutrons to 2.2 Å resolution on the MaNDi neutron diffractometer at the Spallation Neutron Source. The resolution of the neutron data will allow direct determination of the positions of H atoms in the structure, which are believed to be fundamentally important in tuning the individual excitation energies of bacteriochlorophylls in this archetypal photosynthetic antenna complex. This is one of the largest unit-cell systems yet studied using neutron diffraction, and will allow the first high-resolution neutron analysis of a photosynthetic antenna complex.

    • Organizational Affiliation: 

    Neutron Science Directorate, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bacteriochlorophyll a protein
A, B
360Prosthecochloris aestuariiMutation(s): 0 
UniProt
Find proteins for P11741 (Prosthecochloris aestuarii)
Explore P11741 
Go to UniProtKB:  P11741
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11741
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
BCL
Query on BCL
Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
F [auth A]
G [auth A]
C [auth A],
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A],
I [auth A],
M [auth B],
N [auth B],
O [auth B],
P [auth B],
Q [auth B],
R [auth B],
S [auth B]
BACTERIOCHLOROPHYLL A
C55 H74 Mg N4 O6
DSJXIQQMORJERS-AGGZHOMASA-M
SO4
Query on SO4
Download Ideal Coordinates CCD File 
J [auth A]
K [auth A]
L [auth A]
T [auth B]
U [auth B]
J [auth A],
K [auth A],
L [auth A],
T [auth B],
U [auth B],
V [auth B]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.74 Å
  • R-Value Free: 0.159 
  • R-Value Work: 0.132 
  • R-Value Observed: 0.134 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.638α = 90
b = 83.638β = 90
c = 294.781γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Department of Energy (DOE, United States)United StatesDE-SC0001035

Revision History  (Full details and data files)

  • Version 1.0: 2019-03-13
    Type: Initial release
  • Version 1.1: 2019-12-04
    Changes: Author supporting evidence
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references, Derived calculations