1T2L
Three Crystal Structures of Human Coactosin-like Protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | BSRF BEAMLINE 3W1A |
| Synchrotron site | BSRF |
| Beamline | 3W1A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-12 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9813, 0.9816, 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 124.018, 37.033, 60.322 |
| Unit cell angles | 90.00, 106.83, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.800 |
| R-factor | 0.205 |
| Rwork | 0.197 |
| R-free | 0.26900 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.800 |
| Number of reflections | 6039 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 30% PEG400, 0.1M hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
