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1H15

X-ray crystal structure of HLA-DRA1*0101/DRB5*0101 complexed with a peptide from Epstein Barr Virus DNA polymerase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]293
Detector technologyCCD
Collection date2001-02-15
DetectorADSC CCD
Spacegroup nameP 65
Unit cell lengths179.244, 179.244, 92.884
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution19.880 - 3.100
R-factor0.256
Rwork0.256
R-free0.31000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)SINGLE COPY OF 1FV1 (A AND B CHAINS) MINUS PEPTIDE
RMSD bond length0.008
RMSD bond angle26.100

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0003.300
High resolution limit [Å]3.1003.100
Rmerge0.4140.774
Total number of observations166287

*

Number of reflections28750
<I/σ(I)>5.71.1
Completeness [%]94.578.9
Redundancy61.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.4

*

18

*

14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropTris10 (mM)pH7.4
21dropprotein10 (mg/ml)
31reservoirPEG335014 (%)
41reservoirglycine100 (mM)
51reservoirTris10 (mM)pH3.5-4.0

217157

数据于2024-03-13公开中

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