1YLF
X-ray crystal structure of BC1842 protein from Bacillus cereus, a member of the Rrf2 family of putative transcription regulators.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-22 |
Detector | SBC-3 |
Wavelength(s) | 0.97917 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 73.080, 73.080, 157.680 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 2.500 |
R-factor | 0.216 |
Rwork | 0.217 |
R-free | 0.25000 |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.474 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.570 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.101 | 0.517 |
Number of reflections | 17282 | |
<I/σ(I)> | 25.2 | 2.02 |
Completeness [%] | 98.3 | 83.6 |
Redundancy | 17 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.2 M Na Cl, 25% PEG 3350, Tris_Cl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |