2VOF
Structure of mouse A1 bound to the Puma BH3-domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 93 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.640, 60.683, 59.986 |
| Unit cell angles | 90.00, 109.53, 90.00 |
Refinement procedure
| Resolution | 43.980 - 1.800 |
| R-factor | 0.184 |
| Rwork | 0.183 |
| R-free | 0.21000 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.131 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.520 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.040 | 0.160 |
| Number of reflections | 29292 | |
| <I/σ(I)> | 28.2 | 9.6 |
| Completeness [%] | 94.0 | 93.8 |
| Redundancy | 6.4 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.1 M CITRIC ACID.KOH (PH 4.35), 15% PEG 20,000, 0.4 M LICL, 20% GLYCEROL |
