1I1Y
CRYSTAL STRUCTURE OF HUMAN CLASS I MHC (HLA-A2.1) COMPLEXED WITH BETA 2-MICROGLOBULIN AND HIV-RT VARIANT PEPTIDE I1Y
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1997-05-01 |
| Detector | ADSC |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.613, 63.591, 75.326 |
| Unit cell angles | 81.93, 75.94, 78.00 |
Refinement procedure
| Resolution | 15.000 - 2.200 |
| R-factor | 0.244 |
| Rwork | 0.233 |
| R-free | 0.28900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hhh |
| RMSD bond length | 0.010 |
| RMSD bond angle | 2.489 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE (IN CCP4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.073 | 0.231 |
| Total number of observations | 222078 * | |
| Number of reflections | 45024 | |
| <I/σ(I)> | 9.7 | 23.1 |
| Completeness [%] | 97.9 | 96.4 |
| Redundancy | 4.9 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | drop consists of 1:1 mixture of well and protein solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protease | 10 (mg/ml) | |
| 2 | 1 | drop | MES | 25 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 18 (%) | |
| 4 | 1 | reservoir | MES | 25 (mM) |
