1H43
R210E N-TERMINAL LOBE HUMAN LACTOFERRIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 112.900, 57.900, 57.800 |
Unit cell angles | 90.00, 101.40, 90.00 |
Refinement procedure
Resolution | 32.000 * - 2.200 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.23600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lct |
RMSD bond length | 0.006 |
RMSD bond angle | 22.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.058 | 0.300 |
Number of reflections | 18711 | |
<I/σ(I)> | 15.3 | 4.4 |
Completeness [%] | 98.7 | 97 |
Redundancy | 3.4 |
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 |