4LES
2.2 Angstrom Crystal Structure of Conserved Hypothetical Protein 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 | 2013-06-17 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 63 |
Unit cell lengths | 95.754, 95.754, 41.518 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.340 - 2.200 |
R-factor | 0.17693 |
Rwork | 0.175 |
R-free | 0.21151 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.712 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.8.0046) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.052 | 0.522 |
Number of reflections | 11282 | |
<I/σ(I)> | 32.2 | 3.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.4 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 295 | Protein: 7.4 mG/mL, 0.25 M Sodium chloride, 0.01 M Tris-HCL buffer pH 8.3; Screen: JSCG+ (C6), 0.1 M Phosphate-citrate buffer pH 4.2, 40% (v/v) PEG 300, VAPOR DIFFUSION, SITTING DROP, temperature 295K |