3I1H
Crystal structure of human BFL-1 in complex with BAK BH3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-24 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97893 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.236, 43.145, 46.068 |
| Unit cell angles | 90.00, 114.45, 90.00 |
Refinement procedure
| Resolution | 30.070 - 2.200 |
| R-factor | 0.213 |
| Rwork | 0.213 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2voh |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.200 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | AMoRE |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.070 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 0.342 |
| Number of reflections | 7958 | |
| <I/σ(I)> | 6.3 | 2.8 |
| Completeness [%] | 99.7 | 99.7 |
| Redundancy | 3.5 | 3.46 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 298 | 1.5 M sodium malonate, pH 5.8 protein 1.67 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
