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 |