2OUA
Crystal Structure of Nocardiopsis Protease (NAPase)
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 | 2005-01-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 61.605, 61.605, 184.479 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.180 - 1.850 |
Rwork | 0.176 |
R-free | 0.19990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | poly-Ala model of TFPA (to be submitted) |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.180 | |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.097 | 0.469 |
Number of reflections | 34991 | |
<I/σ(I)> | 16.66 | 3.91 |
Completeness [%] | 97.4 | 98.7 |
Redundancy | 5.4 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 1.3M ammonium sulfate, 10%(v/v) dioxane, 0.1M MES, pH 6.0, 10mg/ml NAPase, VAPOR DIFFUSION, HANGING DROP, temperature 298K |