3L6F
Structure of MHC class II molecule HLA-DR1 complexed with phosphopeptide MART-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-30 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 91.210, 135.450, 40.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.220 - 2.100 |
Rwork | 0.212 |
R-free | 0.24940 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1t5w |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.220 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 30332 | |
<I/σ(I)> | 51.3 | 5.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.2 | 14.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.5 | 298 | 20% (w/v) PEG 8000 and 0.1 M sodium cacodylate, pH 6.5, EVAPORATION, temperature 298K |