1JJO
Crystal Structure of Mouse Neuroserpin (Cleaved form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-07-06 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.290, 108.690, 45.990 |
Unit cell angles | 90.00, 101.28, 90.00 |
Refinement procedure
Resolution | 16.890 - 3.060 |
R-factor | 0.232 * |
Rwork | 0.232 |
R-free | 0.30800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | homology model based on all available cleaved serpin structures |
RMSD bond length | 0.008 |
RMSD bond angle | 1.419 |
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] | 17.000 * | 3.100 |
High resolution limit [Å] | 3.060 | 3.060 |
Rmerge | 0.155 * | 0.422 * |
Number of reflections | 9419 | 7975 * |
<I/σ(I)> | 7 | 2 |
Completeness [%] | 79.7 | 74.6 * |
Redundancy | 2.57 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 20 * | 25% PEG8000, 0.2M H2PO4(NH4), 0.1M Tris-HCl, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 25 (%) | |
3 | 1 | reservoir | 0.2 (M) | ||
4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH6.1 |