8Q2B
E. coli Adenylate Kinase variant D158A (AK D158A) showing significant changes to the stacking of catalytic arginine side chains
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-05-02 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 0.87293 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.283, 77.974, 59.911 |
Unit cell angles | 90.00, 93.61, 90.00 |
Refinement procedure
Resolution | 40.080 - 1.760 |
R-factor | 0.1832 |
Rwork | 0.181 |
R-free | 0.22440 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.307 |
Data reduction software | XDS (Oct 15, 2015) |
Data scaling software | Aimless (0.5.25) |
Phasing software | PHASER (2.8.3) |
Refinement software | PHENIX (1.19.2_4158-000) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.450 | 1.820 |
High resolution limit [Å] | 1.760 | 1.760 |
Rmerge | 0.109 | 1.097 |
Rmeas | 0.118 | 1.183 |
Rpim | 0.045 | 0.440 |
Number of reflections | 52176 | 5114 |
<I/σ(I)> | 11.2 | 1.82 |
Completeness [%] | 100.0 | |
Redundancy | 6.9 | 7.1 |
CC(1/2) | 0.998 | 0.627 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | Crystallization: 2 ul of purified AK-D158A at 16.4 mg/ml, mixed with the non-hydrolysable inhibitor Ap5A at a final concentration of 5 mM and 2 ul of precipitant buffer containing 32% PEG 8K, 0.2 M AmSO4, 0.1 M Cacodylate at pH 6.5. |