5FR3
X-ray crystal structure of aggregation-resistant protective antigen of Bacillus anthracis (mutant S559L T576E)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-02-13 |
Detector | DECTRIS PILATUS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 84.547, 94.714, 100.627 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.433 - 1.935 |
R-factor | 0.1798 |
Rwork | 0.178 |
R-free | 0.22720 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1acc |
RMSD bond length | 0.005 |
RMSD bond angle | 0.953 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.450 | 2.040 |
High resolution limit [Å] | 1.940 | 1.940 |
Rmerge | 0.010 | 0.830 |
Number of reflections | 203741 | |
<I/σ(I)> | 8 | 1.4 |
Completeness [%] | 98.7 | 97.2 |
Redundancy | 3.4 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 20 MM MGCL2, 100 MM HEPES PH 7.5, 22% POLY(ACRYLIC ACID SODIUM SALT) 5100 |