3M7U
Crystal Structure of Alpha-Lytic Protease SB1+2 R64A/E182Q 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 | 65.396, 65.396, 79.856 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.196 - 1.050 |
| R-factor | 0.1408 |
| Rwork | 0.141 |
| R-free | 0.16380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ssx |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.109 |
| 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] | 46.196 | 1.050 |
| High resolution limit [Å] | 1.030 | 1.030 |
| Rmerge | 0.120 | 0.644 |
| Number of reflections | 91149 | |
| <I/σ(I)> | 118.4 | 9.5 |
| Completeness [%] | 98.7 | 100 |
| Redundancy | 33.1 | 18.1 |
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 |
