2WFW
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 100.330, 100.330, 88.000 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.600 |
| R-factor | 0.21011 |
| Rwork | 0.208 |
| R-free | 0.24641 |
| Structure solution method | MIR |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.634 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.070 | 0.530 |
| Number of reflections | 64443 | |
| <I/σ(I)> | 14.7 | 3.2 |
| Completeness [%] | 95.2 | 78.6 |
| Redundancy | 7 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 0.05 MM CACL2, 0.1 M BIS-TRIS PH 6.5, 30% PEG550 |
