4RWR
2.1 Angstrom Crystal Structure of Stage II Sporulation Protein D from Bacillus anthracis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-13 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.616, 144.477, 47.076 |
Unit cell angles | 90.00, 115.36, 90.00 |
Refinement procedure
Resolution | 27.530 - 2.100 |
R-factor | 0.19033 |
Rwork | 0.188 |
R-free | 0.24348 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.443 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.105 | 0.623 |
Number of reflections | 32915 | |
<I/σ(I)> | 12.4 | 2.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.3 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | Protein: 6.7 mG/mL, 0.5 M Sodium chloride, 0.01 M Tris-HCL buffer, pH 8.3, 2mM N-Acetylglucosamine; Screen: Classics II (H7), 0.15M DL-Malic acid, pH 7.0, 20% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |