1I04
CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN-I FROM MOUSE LIVER
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1997-08-15 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.840, 60.840, 100.290 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.219 |
| Rwork | 0.219 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mup |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.355 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.060 | 0.276 |
| Total number of observations | 48342 * | |
| Number of reflections | 14762 | |
| <I/σ(I)> | 17.2 | 3.3 |
| Completeness [%] | 97.9 | 85.9 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 50-70% ammonium sulfate, citrate, phosphate buffer, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 50-70 (%) | |
| 2 | 1 | reservoir | citrate/phophosphate | 100 (mM) |
