5IE9
Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
Synchrotron site | PAL/PLS |
Beamline | 7A (6B, 6C1) |
Temperature [K] | 83 |
Detector technology | CCD |
Collection date | 2014-05-11 |
Detector | ADSC QUANTUM 1 |
Wavelength(s) | 0.9798 |
Spacegroup name | P 32 |
Unit cell lengths | 90.578, 90.578, 97.056 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.800 |
R-factor | 0.2232 |
Rwork | 0.222 |
R-free | 0.25370 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gta |
RMSD bond length | 0.008 |
RMSD bond angle | 1.318 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.870 |
High resolution limit [Å] | 2.770 | 2.800 |
<I/σ(I)> | 2 | |
Completeness [%] | 98.7 | 89.4 |
Redundancy | 3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.1mM sodium cacodylate pH 6.5, 1M sodium citrate |