8E2Z
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 | 50.742, 81.388, 110.985 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.840 - 1.130 |
| R-factor | 0.19061 |
| Rwork | 0.189 |
| R-free | 0.21701 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6p2s |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.403 |
| 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] | 99.000 | 99.000 | 1.160 |
| High resolution limit [Å] | 1.070 | 2.910 | 1.130 |
| Rmerge | 0.025 | 0.027 | 0.005 |
| Rmeas | 0.036 | 0.038 | 0.005 |
| Rpim | 0.025 | 0.027 | 0.005 |
| Total number of observations | 328562 | ||
| Number of reflections | 196900 | 9121 | 9940 |
| <I/σ(I)> | 20 | ||
| Completeness [%] | 98.3 | 86.2 | 100 |
| Redundancy | 1.7 | 1.9 | 1 |
| CC(1/2) | 0.992 | 0.981 | 0.949 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 277 | 0.2 M ammonium acetate, 15% PEG 4000, 0.1 M sodium citrate, pH5.6, |
