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8F7Z

VRC34.01_mm28 bound to fusion peptide

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyPIXEL
Collection date2022-02-10
DetectorDECTRIS EIGER X 16M
Wavelength(s)1.000
Spacegroup nameP 21 21 21
Unit cell lengths129.850, 130.554, 130.589
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution36.220 - 2.700
R-factor0.2116
Rwork0.210
R-free0.24280
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)Alphafold model
RMSD bond length0.006
RMSD bond angle0.973
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHENIX
Refinement softwarePHENIX ((1.20.1_4487: ???))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.750
High resolution limit [Å]2.7002.700
Rmerge0.1340.581
Rmeas0.1460.629
Rpim0.0570.238
Number of reflections604343015
<I/σ(I)>162.6
Completeness [%]97.8
Redundancy6.5
CC(1/2)0.9910.844
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP29310% PEG 3350, 1.4M Na/K Phosphate pH 7.5

219869

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