1UHN
The crystal structure of the calcium binding protein AtCBL2 from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-09-28 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.02 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 83.900, 118.100, 49.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.580 * - 2.100 |
| R-factor | 0.206 |
| Rwork | 0.204 |
| R-free | 0.24800 |
| Structure solution method | MIR |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.415 * |
| Data reduction software | Crystal (Clear) |
| Data scaling software | CrystalClear ((MSC/RIGAKU)) |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.1.27) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.900 | 2.170 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.055 | 0.266 |
| Total number of observations | 80068 * | |
| Number of reflections | 14399 | |
| <I/σ(I)> | 8.5 | 1.9 |
| Completeness [%] | 98.0 | 96.3 |
| Redundancy | 5.6 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 277 * | Nagae, M., (2003) Acta Crystallogr., D59, 1079. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 5 (mM) | pH7.5 |
| 2 | 1 | drop | 100 (mM) | ||
| 3 | 1 | drop | dithiothreitol | 1 (mM) | |
| 4 | 1 | drop | 1 (mM) | ||
| 5 | 1 | drop | protein | 6 (mg/ml) | |
| 6 | 1 | reservoir | sodium MES | 0.1 (M) | pH6.0 |
| 7 | 1 | reservoir | 0.2 (M) | ||
| 8 | 1 | reservoir | PEG8000 | 10 (%) |
