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 |
Collection date | 2000-05-01 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.380, 80.120, 99.930 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 193.800 * - 1.700 |
R-factor | 0.197 * |
Rwork | 0.197 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | THEORETICAL MODEL |
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] | 20.100 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.096 | 0.409 |
Total number of observations | 177455 * | |
Number of reflections | 33538 | |
<I/σ(I)> | 14 | 2.8 |
Completeness [%] | 99.4 | 96.6 |
Redundancy | 5.3 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | PEG 400 , Mn(CH3COO)2 , DMSO, Tris-HCl, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 100 (mg/ml) | |
2 | 1 | reservoir | PEG400 | ||
3 | 1 | reservoir | 0.03 (M) | ||
4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH7.5 |