3ROE
Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Thymidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-22 |
| Detector | MARMOSAIC 300 |
| Wavelength(s) | 1.12712 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.209, 124.446, 164.249 |
| Unit cell angles | 90.00, 102.71, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.110 |
| R-factor | 0.17823 |
| Rwork | 0.177 |
| R-free | 0.21060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o8n |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.730 |
| 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 | 2.150 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.087 | 0.593 |
| Number of reflections | 477756 | |
| <I/σ(I)> | 26.826 | 2.568 |
| Completeness [%] | 97.6 | 83.3 |
| Redundancy | 4.1 | 3.6 |
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 |
