7MWC
ERAP1 binds peptide C-terminus of a LPF sequence (AAAAFKARKF)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-03-01 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.030, 66.680, 121.710 |
| Unit cell angles | 90.07, 101.81, 90.05 |
Refinement procedure
| Resolution | 55.120 - 3.000 |
| R-factor | 0.244 |
| Rwork | 0.238 |
| R-free | 0.29800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rjo |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.627 |
| Data reduction software | iMOSFLM |
| Data scaling software | pointless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 58.200 | 3.200 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Number of reflections | 31557 | 4503 |
| <I/σ(I)> | 7.6 | 2.4 |
| Completeness [%] | 90.0 | 87.5 |
| Redundancy | 2.25 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 100mM Tris, pH 8.5, 12% w/v PEG8000 |
