1AEW
L-CHAIN HORSE APOFERRITIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 290 |
Detector technology | IMAGE PLATE |
Collection date | 1993-02 |
Detector | MARRESEARCH |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 184.000, 184.000, 184.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.950 |
R-factor | 0.192 |
Rwork | 0.192 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HORSE SPLEEN L FERRITIN. |
RMSD bond length | 0.008 |
RMSD bond angle | 14.940 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Refinement software | TNT (5D) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.030 | 0.120 |
Number of reflections | 19915 | |
<I/σ(I)> | 17.6 | 6.3 |
Completeness [%] | 100.0 | 97.5 |
Redundancy | 7.6 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | CRYSTALLIZED BY SITTING DROP: 15 LAMBDA PROTEIN + 1-2 LAMBDA 2% CDSO4, pH 7.0, vapor diffusion - sitting drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | 0.015 ml |
2 | 1 | drop | 2 (%) | 0.001-0.002 ml |