2FHA
HUMAN H CHAIN FERRITIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 293 |
Detector technology | FILM |
Collection date | 1988-11-14 |
Detector | KODAK |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 184.800, 184.800, 184.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
R-factor | 0.186 |
Rwork | 0.186 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fha |
RMSD bond length | 0.007 |
RMSD bond angle | 15.192 * |
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] | 1.900 | 1.900 |
Rmerge | 0.076 | 0.567 |
Number of reflections | 20238 | |
<I/σ(I)> | 9 | 2.4 |
Completeness [%] | 94.0 | 90 |
Redundancy | 7.2 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 0.08% CACL2 / 15% MPD IN 50 MM HEPES BUFFER PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.5-5 (mg/ml) | |
2 | 1 | drop | 0.04 (%(w/v)) | ||
3 | 1 | drop | MPD | 7.5 (%) | |
4 | 1 | drop | HEPES | 25 (mM) | |
5 | 1 | reservoir | MPD | 10-15 (%) |