8EC5
Structures of HLA-B8E76C loaded with long peptides reveal novel features at the N-terminus of the groove
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2020-08-09 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.758, 81.149, 110.580 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.000 - 1.220 |
| R-factor | 0.1995 |
| Rwork | 0.199 |
| R-free | 0.21220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6p2s |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.948 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.240 |
| High resolution limit [Å] | 1.220 | 3.310 | 1.220 |
| Rmerge | 0.072 | 0.048 | 0.672 |
| Rmeas | 0.076 | 0.053 | 0.716 |
| Rpim | 0.026 | 0.020 | 0.244 |
| Total number of observations | 1207616 | ||
| Number of reflections | 133304 | 6138 | 6699 |
| <I/σ(I)> | 10.6 | ||
| Completeness [%] | 98.5 | 85.3 | 99.9 |
| Redundancy | 9.1 | 6.8 | 8.1 |
| CC(1/2) | 0.996 | 0.879 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 5.8 | 298 | 0.2 M ammonium acetate, 15% PEG 10000, 0.1 M sodium citrate |
