1CE2
STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 303 |
Detector technology | IMAGE PLATE |
Collection date | 1997-02 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 77.462, 91.035, 131.507 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.500 |
R-factor | 0.187 * |
Rwork | 0.187 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | BUFFALO LACTOFERRIN (1BIY) |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.660 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.069 | 0.194 * |
Number of reflections | 29307 | |
<I/σ(I)> | 15 | 4.08 |
Completeness [%] | 90.0 | 76.1 |
Redundancy | 1.8 | 1.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 8 | 303 * | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 50-70 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 0.025 (M) | |
3 | 1 | 2 | ethanol | 19 (%(v/v)) |