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4BF3

ErpC, a member of the complement regulator acquiring family of surface proteins from Borrelia burgdorfei, possesses an architecture previously unseen in this protein family.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsDIAMOND BEAMLINE I03
Synchrotron siteDiamond
BeamlineI03
Temperature [K]120
Detector technologyPIXEL
Collection date2011-12-02
DetectorDECTRIS PILATUS 6M
Spacegroup nameP 21 21 21
Unit cell lengths62.520, 68.160, 76.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution24.150 - 2.370
R-factor0.1917
Rwork0.190
R-free0.23020
Structure solution methodSAD
Starting model (for MR)NONE
RMSD bond length0.010
RMSD bond angle1.180
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwareautoSHARP
Refinement softwareBUSTER (2.11.4)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]24.1502.460
High resolution limit [Å]2.3702.370
Rmerge0.0700.780
Number of reflections13663
<I/σ(I)>13.72.6
Completeness [%]99.799.9
Redundancy5.35.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
127% (W/V) PEG 2000 MME, 0.1M SODIUM CACODYLATE PH 6.5

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