2A33
X-Ray Structure of a Lysine Decarboxylase-Like Protein from Arabidopsis Thaliana Gene AT2G37210
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-13 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.403, 66.773, 98.639 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.984 - 1.950 |
| R-factor | 0.183 |
| Rwork | 0.181 |
| R-free | 0.23400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ydh |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.712 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.100 | 0.518 |
| Number of reflections | 26424 | |
| <I/σ(I)> | 15.009 | 1.756 |
| Completeness [%] | 99.8 | 98.6 |
| Redundancy | 10.7 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 296 | 10 MG/ML PROTEIN, 22% PEG 2K, 0.084 M MAGNESIUM SULFATE, 0.100 M BISTRIS, vapor diffusion, hanging drop, temperature 296K, pH 6.50 |
