3M7T
Crystal Structure of Alpha-Lytic Protease SB2+3 E8A/R105S Mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.11588 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 66.015, 66.015, 79.749 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.008 - 1.550 |
| R-factor | 0.1382 |
| Rwork | 0.136 |
| R-free | 0.20200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ssx |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.905 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX (dev_328) |
| Refinement software | PHENIX ((phenix.refine: dev_328)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.171 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.100 | 0.457 |
| Number of reflections | 29042 | |
| <I/σ(I)> | 36.575 | 4.676 |
| Completeness [%] | 97.7 | 100 |
| Redundancy | 10.5 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 277 | 1.3 M lithium sulfate, 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
