3URC
T181G mutant of alpha-Lytic Protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-08-30 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.79 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 65.645, 65.645, 79.627 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.770 - 1.100 |
R-factor | 0.11674 |
Rwork | 0.115 |
R-free | 0.13640 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 1.683 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.130 |
High resolution limit [Å] | 1.100 | 1.100 |
Number of reflections | 78364 | |
<I/σ(I)> | 24.7 | 3 |
Completeness [%] | 99.9 | 99.6 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 1.3 M lithium sulfate and 20 mM Tris sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |