4AF8
The structural basis for metacaspase substrate specificity and activation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-14 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 78.372, 50.115, 85.400 |
| Unit cell angles | 90.00, 117.09, 90.00 |
Refinement procedure
| Resolution | 76.030 - 1.400 |
| R-factor | 0.15389 |
| Rwork | 0.153 |
| R-free | 0.17767 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PARIALLY-REFINED SEMET DERIVATIVE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.178 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | Auto-Rickshaw |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.700 | 1.480 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.040 | 0.220 |
| Number of reflections | 56770 | |
| <I/σ(I)> | 20.3 | 4.4 |
| Completeness [%] | 97.6 | 84.8 |
| Redundancy | 3.5 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 50 MM HEPES PH 7.0, 0.1% TRYPTONE, 20% PEG 3350 |
