5E1B
Crystal structure of NRMT1 in complex with SPKRIA peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-24 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 107.259, 107.259, 205.416 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.540 - 1.650 |
| R-factor | 0.1517 |
| Rwork | 0.151 |
| R-free | 0.17590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdbid 2ex4 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.815 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.12) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.010 | 47.540 | 1.630 |
| High resolution limit [Å] | 1.600 | 8.760 | 1.600 |
| Rmerge | 0.134 | 0.044 | 1.213 |
| Rmeas | 0.137 | 0.045 | 1.241 |
| Rpim | 0.029 | 0.011 | 0.265 |
| Total number of observations | 2000468 | 11627 | 97692 |
| Number of reflections | 92380 | ||
| <I/σ(I)> | 21.7 | 59.6 | 3.2 |
| Completeness [%] | 100.0 | 99.5 | 100 |
| Redundancy | 21.7 | 16.4 | 21.8 |
| CC(1/2) | 0.999 | 0.999 | 0.869 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 26% PEG3350, 16% tacsimate |
