1CB6
STRUCTURE OF HUMAN APOLACTOFERRIN AT 2.0 A RESOLUTION.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS |
| Synchrotron site | SRS |
| Temperature [K] | 295 |
| Detector technology | FILM |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 152.090, 94.580, 55.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| R-factor | 0.201 |
| R-free | 0.28600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1LGF (LACTOFERRIN) |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.700 * |
| Data reduction software | MOSFLM |
| Phasing software | CCP4 ((ALMN)) |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.000 | 2.120 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.083 | 0.610 |
| Number of reflections | 53450 | |
| <I/σ(I)> | 30.3 | 2.7 |
| Completeness [%] | 92.0 | 91 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microdialysis * | 7.8 | pH 7.8 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 12 (mg/ml) | |
| 2 | 1 | 2 | Tris-HCl | 0.05 (M) | |
| 3 | 1 | 2 | MPD | 5 (%(v/v)) | |
| 4 | 1 | 2 | absolute ethanol | 5 (%(v/v)) |






