1H76
The crystal structure of diferric porcine serum transferrin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Detector | MAR scanner 300 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 223.770, 44.890, 78.860 |
Unit cell angles | 90.00, 105.39, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.150 |
R-factor | 0.136 * |
Rwork | 0.136 |
R-free | 0.18200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 0TFD |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.890 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0.32) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.310 * | 2.200 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.073 | 0.123 |
Total number of observations | 145143 * | |
Number of reflections | 41503 | |
<I/σ(I)> | 15.7 | 8.1 |
Completeness [%] | 96.0 | 97.4 |
Redundancy | 3.6 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8.5 | 277 * | pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 120 (mg/ml) | in water |
2 | 1 | 1 | PEG4000 | 20 (%(w/v)) | |
3 | 1 | 1 | 0.2 (M) | ||
4 | 1 | 1 | Tris-HCl | 0.1 (M) |