6QFM
Structure of human Mcl-1 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 | 2007-12-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.973 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.042, 58.345, 76.922 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 9.980 - 2.000 |
| R-factor | 0.2051 |
| Rwork | 0.202 |
| R-free | 0.26110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nl9 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.281 |
| 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] | 25.000 | 25.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 4.300 | 2.000 |
| Rmerge | 0.079 | 0.042 | 0.355 |
| Total number of observations | 31218 | ||
| Number of reflections | 9678 | 1181 | 448 |
| <I/σ(I)> | 10.4 | ||
| Completeness [%] | 84.8 | 94.3 | 40.4 |
| Redundancy | 3.2 | 3.3 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 100 mM imidazole buffer pH 7.0, 50 mM zinc acetate and 20-25% polyethylene glycol (PEG) 3350 |
