Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1997-03-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 85.175, 99.496, 103.052 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.620 |
R-factor | 0.194 * |
Rwork | 0.194 |
R-free | 0.26400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HUMAN LACTOFERRIN |
RMSD bond length | 0.012 |
RMSD bond angle | 2.000 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.780 |
High resolution limit [Å] | 2.620 | 2.620 |
Rmerge | 0.063 | 0.250 |
Number of reflections | 25558 | |
<I/σ(I)> | 28.7 | 5.29 |
Completeness [%] | 95.3 | 80 * |
Redundancy | 3.87 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 8.5 | 6 * | 40MG/ML PROTEIN IN 10MM TRIS HCL, PH 8.5, MICRODIALYSED AGA AT 6 DEGREES CELSIUS |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20-30 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 0.025 (M) | |
3 | 1 | 2 | ethanol | 10 (%(v/v)) |