3ROX
Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-11 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 125.849, 125.849, 116.368 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.400 |
| R-factor | 0.18 |
| Rwork | 0.177 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o8n |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.786 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 (MOLREP) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.390 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.089 | 0.498 |
| Number of reflections | 97986 | |
| <I/σ(I)> | 42.447 | 5.677 |
| Completeness [%] | 94.9 | 100 |
| Redundancy | 6.9 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 0.1 M SODIUM ACETATE, 1.5 M AMMONIUM SULFATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
