1F9N
CRYSTAL STRUCTURE OF AHRC, THE ARGININE REPRESSOR/ACTIVATOR PROTEIN FROM BACILLUS SUBTILIS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1995-11-04 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 230.310, 73.860, 138.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.700 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.27000 |
RMSD bond length | 0.004 |
RMSD bond angle | 1.000 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | AMoRE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.870 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.066 | 0.140 |
Number of reflections | 28055 | |
<I/σ(I)> | 10 | |
Completeness [%] | 88.7 | 85.7 |
Redundancy | 1.6 | 1.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.9 | 291 | PEG 4000, ammonium sulphate, phosphate buffer, protease inhibitors (PMSF, TPCK) in isopropanol, pH 4.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 60 (mM) | |
3 | 1 | reservoir | phosphate | 100 (mM) | pH4.9 |
4 | 1 | reservoir | PEG4000 | 3 (%(w/v)) |