5F2H
2.75 Angstrom resolution crystal structure of uncharacterized protein from Bacillus cereus ATCC 10987
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-27 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.067, 42.176, 106.032 |
Unit cell angles | 90.00, 92.45, 90.00 |
Refinement procedure
Resolution | 27.170 - 2.750 |
R-factor | 0.23319 |
Rwork | 0.230 |
R-free | 0.29052 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.511 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.800 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.097 | 0.634 |
Number of reflections | 16616 | |
<I/σ(I)> | 31 | 3.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.4 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | Protein (SeMet): 8.9 mg/ml in 10 mM Tris-HCl pH 8.3 0.25 M NaCl, 5 mM BME Crystallization: The Classics II D7(43): 0.1 M Bis-Tris pH 6.5, 25% (w/v) PEG3350 Cryo: Crystallization condition soak |