3PH9
Crystal structure of the human anterior gradient protein 3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-11 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.934 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.290, 71.450, 59.810 |
| Unit cell angles | 90.00, 97.72, 90.00 |
Refinement procedure
| Resolution | 45.620 - 1.830 |
| R-factor | 0.17968 |
| Rwork | 0.177 |
| R-free | 0.23260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sen |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.396 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.830 |
| Rmerge | 0.108 |
| Number of reflections | 24330 |
| <I/σ(I)> | 15.5 |
| Completeness [%] | 99.0 |
| Redundancy | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295.15 | 25 % PEG 4000, 0.2 M MgCl2, 0.2 M NaCl, 0.1 M Tris-Cl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.15K |
