1H45
R210G N-TERMINAL LOBE HUMAN LACTOFERRIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 131.720, 58.890, 57.530 |
Unit cell angles | 90.00, 114.38, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.950 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.24700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lct |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.053 | 0.146 |
Number of reflections | 27857 | |
<I/σ(I)> | 13.6 | 4.2 |
Completeness [%] | 94.2 | 60.4 |
Redundancy | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8 | 4 * | HEPES, NACL, pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 28 (mg/ml) | |
2 | 1 | 1 | HEPES | 20 (mM) | |
3 | 1 | 1 | 1 (M) | pH8.0 |