5NE8
Crystal structure of H307A mutant of Thermotoga maritima TmPEP1050 aminopeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 2 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-11-25 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.9801 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.790, 138.650, 61.250 |
Unit cell angles | 90.00, 110.51, 90.00 |
Refinement procedure
Resolution | 40.107 - 1.750 |
R-factor | 0.1686 |
Rwork | 0.165 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4p6y |
RMSD bond length | 0.012 |
RMSD bond angle | 1.263 |
Data reduction software | XDS (20160617) |
Data scaling software | XSCALE (20160617) |
Phasing software | PHASER (2.6.0) |
Refinement software | PHENIX (1.10.1-2155) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.107 | 40.107 | 1.790 |
High resolution limit [Å] | 1.750 | 7.820 | 1.750 |
Rmerge | 0.056 | 0.034 | 0.563 |
Rmeas | 0.060 | 0.037 | 0.609 |
Number of reflections | 67094 | 772 | 4879 |
<I/σ(I)> | 17.96 | 43.73 | 2.38 |
Completeness [%] | 99.5 | 98.3 | 97.2 |
Redundancy | 6.732 | 6.911 | 6.786 |
CC(1/2) | 0.999 | 0.997 | 0.841 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 292 | TmPep1050 H307A (230 uM) was crystallised in 0.1 M sodium citrate 10 % PEG3350 pH4.5 |