3RJO
Crystal Structure of ERAP1 Peptide Binding Domain
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 | 2006-11-05 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.840, 67.310, 65.920 |
| Unit cell angles | 90.00, 110.25, 90.00 |
Refinement procedure
| Resolution | 53.200 - 2.300 |
| R-factor | 0.19589 |
| Rwork | 0.192 |
| R-free | 0.26231 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.047 |
| RMSD bond angle | 2.113 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 100.000 | 100.000 | 2.590 |
| High resolution limit [Å] | 2.300 | 5.390 | 2.300 |
| Rmerge | 0.104 | 0.051 | 0.227 |
| Number of reflections | 23337 | ||
| <I/σ(I)> | 10.8 | ||
| Completeness [%] | 94.4 | 99.1 | 70.9 |
| Redundancy | 2.9 | 3.6 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 298 | 12% PEG 6000, 0.2M MgCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
