6AFY
Proton pyrophosphatase-E225S mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL15A1 |
Synchrotron site | NSRRC |
Beamline | BL15A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-12-19 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 218.124, 88.194, 158.956 |
Unit cell angles | 90.00, 125.38, 90.00 |
Refinement procedure
Resolution | 21.798 - 2.401 |
R-factor | 0.1922 |
Rwork | 0.191 |
R-free | 0.22580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4a01 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.173 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.490 |
High resolution limit [Å] | 2.400 | 5.160 | 2.400 |
Rmerge | 0.091 | 0.031 | 1.145 |
Rmeas | 0.107 | 0.036 | 1.347 |
Rpim | 0.055 | 0.018 | 0.703 |
Total number of observations | 311053 | ||
Number of reflections | 87932 | 9606 | 7771 |
<I/σ(I)> | 10.6 | ||
Completeness [%] | 91.7 | 98.2 | 81.6 |
Redundancy | 3.5 | 3.9 | 3.3 |
CC(1/2) | 0.998 | 0.657 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 100 mM MES (pH 6.5), 250 mM MgCl2, 23% (w/v) PEG2KMME and 10% glycerol |