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3BEV

11mer Structure of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]100
Detector technologyCCD
Collection date2004-11-07
DetectorMACSCIENCE
Wavelength(s)0.97904
Spacegroup nameP 21 21 21
Unit cell lengths71.306, 72.199, 72.711
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.950 - 2.100
R-factor0.233
Rwork0.230
R-free0.28600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ogt
RMSD bond length0.012
RMSD bond angle2.327
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.170
High resolution limit [Å]2.1002.100
Rmerge0.1430.650
Number of reflections22499
<I/σ(I)>17.13.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP729327% PEG 3350, 0.1M HEPES pH7.0, 0.1M MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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