4IJO
Unraveling hidden allosteric regulatory sites in structurally homologues metalloproteases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | OXFORD DIFFRACTION ENHANCE ULTRA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-24 |
| Detector | OXFORD ONYX CCD |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 50.435, 60.164, 53.777 |
| Unit cell angles | 90.00, 114.80, 90.00 |
Refinement procedure
| Resolution | 25.600 - 1.900 |
| R-factor | 0.18784 |
| Rwork | 0.183 |
| R-free | 0.23194 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y93 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.804 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.600 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.116 | 0.392 |
| Number of reflections | 10933 | |
| <I/σ(I)> | 5.5 | 2 |
| Completeness [%] | 94.3 | 71.5 |
| Redundancy | 5.7 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1 M Tris-HCl, 30% PEG 6000, 200mM AHA, 1.0M LiCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
