4O03
Crystal structure of Ca2+ bound prothrombin deletion mutant residues 146-167
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-06-28 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 177.459, 89.431, 87.982 |
| Unit cell angles | 90.00, 116.36, 90.00 |
Refinement procedure
| Resolution | 39.750 - 3.380 |
| R-factor | 0.23539 |
| Rwork | 0.233 |
| R-free | 0.27942 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nzq |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.650 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP (from ccp4) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.830 | 3.460 |
| High resolution limit [Å] | 3.380 | 3.740 | 3.380 |
| Rmerge | 0.128 | 0.270 | 0.430 |
| Number of reflections | 16635 | ||
| <I/σ(I)> | 6.9 | 3.6 | 2 |
| Completeness [%] | 95.8 | 94.6 | 92.4 |
| Redundancy | 2.9 | 2.6 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 100 mM HEPES, pH 7.5, 10% PEG 4000 and 5% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
