6JD9
Proteus mirabilis lipase mutant - I118V/E130G
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE TPS 05A |
Synchrotron site | NSRRC |
Beamline | TPS 05A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-08-16 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 1.00 |
Spacegroup name | P 32 |
Unit cell lengths | 65.310, 65.310, 63.591 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.850 - 1.580 |
R-factor | 0.14 |
Rwork | 0.139 |
R-free | 0.16260 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.026 |
RMSD bond angle | 2.353 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.5.17) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 63.590 | 63.590 | 1.610 |
High resolution limit [Å] | 1.580 | 8.650 | 1.580 |
Rmerge | 0.082 | 0.090 | 0.130 |
Rmeas | 0.091 | 0.105 | 0.144 |
Rpim | 0.039 | 0.052 | 0.061 |
Number of reflections | 41629 | 252 | 2059 |
<I/σ(I)> | 16.3 | ||
Completeness [%] | 100.0 | 97.5 | 100 |
Redundancy | 5.7 | 4.7 | 5.5 |
CC(1/2) | 0.992 | 0.891 | 0.982 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.1 M HEPES pH 7.5, 70% MPD |