3RO7
Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Thymine.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97935 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 126.291, 126.291, 109.472 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.500 |
| R-factor | 0.178 |
| Rwork | 0.175 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o8n |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.659 |
| 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 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.162 | 0.746 |
| Number of reflections | 125076 | |
| <I/σ(I)> | 21.875 | 2.694 |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 10.7 | 9.7 |
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 273K, temperature 293K |
