7E43
Structural insights into a bifunctional peptide methionine sulfoxide reductase MsrA/B fusion protein from Helicobacter pylori
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 11C |
Synchrotron site | PAL/PLS |
Beamline | 11C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-07-14 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 52.125, 72.505, 82.230 |
Unit cell angles | 93.16, 93.80, 111.08 |
Refinement procedure
Resolution | 27.590 - 2.200 |
R-factor | 0.1889 |
Rwork | 0.188 |
R-free | 0.21410 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3e0m |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.240 |
High resolution limit [Å] | 2.200 | 5.960 | 2.200 |
Rmerge | 0.063 | 0.048 | 0.179 |
Rmeas | 0.074 | 0.057 | 0.223 |
Rpim | 0.040 | 0.031 | 0.131 |
Total number of observations | 163323 | ||
Number of reflections | 53424 | 2565 | 2417 |
<I/σ(I)> | 16.4 | ||
Completeness [%] | 94.1 | 90.3 | 86.6 |
Redundancy | 3.1 | 3.3 | 2.3 |
CC(1/2) | 0.993 | 0.909 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.1 M sodium acetate pH 4.6 and 2.0 M sodium formate |