1LB3
Structure of recombinant mouse L chain ferritin at 1.2 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE DW32 |
Synchrotron site | LURE |
Beamline | DW32 |
Temperature [K] | 150 |
Detector technology | IMAGE PLATE |
Collection date | 2000-04-17 |
Detector | MARRESEARCH |
Wavelength(s) | 0.966 |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 180.590, 180.590, 180.590 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.000 - 1.210 |
R-factor | 0.1335 |
Rwork | 0.132 |
R-free | 0.16000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h96 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.690 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXL-97 |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.000 | 1.250 |
High resolution limit [Å] | 1.210 | 1.210 |
Rmerge | 0.078 * | 0.602 * |
Total number of observations | 399787 * | |
Number of reflections | 74509 | 5144 * |
<I/σ(I)> | 6.4 | 2 |
Completeness [%] | 98.4 | 98.4 |
Redundancy | 5.5 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 * | Granier, T., (2001) Acta Crystallogr., D57, 1491. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3.5 (mg/ml) | |
2 | 1 | drop | Tris | 20 (mM) | pH7.4 |
3 | 1 | reservoir | ammonium sulfate | 0.92 (M) | |
4 | 1 | reservoir | 0.4 (%) | ||
5 | 1 | reservoir | 3 (mM) |