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4DAG

Structure of the Human Metapneumovirus Fusion Protein with Neutralizing Antibody Identifies a Pneumovirus Antigenic Site

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.3.1
Synchrotron siteALS
Beamline8.3.1
Temperature [K]112
Detector technologyCCD
Collection date2008-10-01
DetectorADSC QUANTUM 315r
Wavelength(s)1.000
Spacegroup nameP 63 2 2
Unit cell lengths258.960, 258.960, 167.360
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution44.853 - 3.390
R-factor0.2613
Rwork0.260
R-free0.28950
Structure solution methodMIR
Starting model (for MR)B20-4 Fab model PDB ENTRY 2FJH
RMSD bond length0.011
RMSD bond angle1.674
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareSHARP
Refinement softwarePHENIX ((phenix.refine: 1.7.1_743))
Data quality characteristics
 Overall
Low resolution limit [Å]224.000
High resolution limit [Å]3.200
Rmerge0.179
Number of reflections36420
Completeness [%]72.7
Redundancy6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.629316% PEG 5000 MME, 15% Glycerol, 100 mM Citrate pH 5.6. Crystals appeared after 7-15 days with two distinct morphologies: a square-like crystal and a longer, pointed crystal form., VAPOR DIFFUSION, HANGING DROP, temperature 293K

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