6QG8
Structure of human Bcl-2 in complex with PUMA BH3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.135, 54.950, 84.725 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.1713 |
| Rwork | 0.169 |
| R-free | 0.21630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yxj |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.485 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 3.880 | 1.800 |
| Rmerge | 0.111 | 0.056 | 0.534 |
| Total number of observations | 47632 | ||
| Number of reflections | 13577 | 1797 | 294 |
| <I/σ(I)> | 7.1 | ||
| Completeness [%] | 75.0 | 91.9 | 16.7 |
| Redundancy | 3.5 | 3.6 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 284 | from 0.2M MgCl2, 25% PegMME 2k, 0.1M Na Acetate buffer pH 5.5 |
