2BKQ
NEDD8 protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.070, 57.510, 74.996 |
| Unit cell angles | 99.74, 110.95, 92.41 |
Refinement procedure
| Resolution | 69.010 - 2.000 |
| R-factor | 0.196 |
| Rwork | 0.193 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.509 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.050 | 0.250 |
| Number of reflections | 54875 | |
| <I/σ(I)> | 9.8 | 3 |
| Completeness [%] | 96.7 | 95.7 |
| Redundancy | 2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | NEDP1 (14MG/ML) WITH EQUAL VOLUME OF RESERVOIR SOLUTION CONTAINING 0.1M BICINE PH9.0, 30% PEG3000., pH 9.00 |
