1LT1
SLIDING HELIX INDUCED CHANGE OF COORDINATION GEOMETRY IN A MODEL DI-MN(II) PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.200 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.225, 89.270, 146.288 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.910 |
| R-factor | 0.20367 |
| Rwork | 0.201 |
| R-free | 0.24400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AB DIMER FROM THE STRUCTURE 1JM0 |
| RMSD bond length | 0.030 |
| RMSD bond angle | 2.220 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 6.030 | 2.010 |
| High resolution limit [Å] | 1.910 | 1.910 |
| Rmerge | 0.125 | 0.463 |
| Total number of observations | 94932 * | |
| Number of reflections | 38634 | |
| <I/σ(I)> | 6.9 | 2.1 |
| Completeness [%] | 96.6 | 96.6 |
| Redundancy | 2.5 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | PEG400, MANGANESE ACETATE, BUFFER TRIS, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG400 | 34 (%) | |
| 3 | 1 | reservoir | 0.03 (M) | ||
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH7.5 |
