4NZQ
Crystal structure of Ca2+-free 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 | 2013-05-29 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 88.754, 171.739, 141.252 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.227 - 2.807 |
| R-factor | 0.22819 |
| Rwork | 0.226 |
| R-free | 0.27891 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB entries 3NXP and 2PF1 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.743 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (from ccp4) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.150 | 2.850 |
| High resolution limit [Å] | 2.800 | 3.080 | 2.800 |
| Rmerge | 0.098 | 0.326 | 0.479 |
| Number of reflections | 26373 | ||
| <I/σ(I)> | 13.8 | 4.2 | 2.5 |
| Completeness [%] | 98.5 | 96.7 | 96.7 |
| Redundancy | 5.8 | 4.6 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 100 mM Tris-HCl, pH 8.5 and 30% PEG300, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
