3MAL
Crystal structure of the SDF2-like protein from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 61 |
| Unit cell lengths | 96.130, 96.130, 69.343 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 53.300 - 1.950 |
| R-factor | 0.16921 |
| Rwork | 0.167 |
| R-free | 0.21279 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t9f |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.506 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.300 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.116 | 0.380 |
| Number of reflections | 26693 | |
| <I/σ(I)> | 14 | 3.7 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 5.5 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 293 | 0.1 M Hepes, 0.2 M ammonium sulphate, 22.5% (w/v) PEG 3350, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
