3NQZ
Crystal structure of the autoprocessed Vibriolysin MCP-02 with E369A mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ DW |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-02-06 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.48 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 82.535, 82.535, 154.206 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 16.970 - 2.050 |
R-factor | 0.18105 |
Rwork | 0.179 |
R-free | 0.21991 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nqx |
RMSD bond length | 0.016 |
RMSD bond angle | 1.613 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 16.970 | 2.100 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.073 | 0.453 |
Number of reflections | 36839 | |
<I/σ(I)> | 20 | 30 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.6 | 16.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 9% PEG 10000, Tris buffer, 0.01M NiCl2 , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |