9GUG
Crystal structure of NtcA from S. elongatus in apo form A1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-17 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.977 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 95.167, 95.487, 160.788 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.790 - 2.700 |
R-factor | 0.24295 |
Rwork | 0.241 |
R-free | 0.27709 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.776 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 80.400 | 2.790 |
High resolution limit [Å] | 2.650 | 2.650 |
Number of reflections | 21137 | 21137 |
<I/σ(I)> | 5.8 | |
Completeness [%] | 98.0 | 98 |
Redundancy | 3.5 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 294.15 | NtcA protein was at 6,1 mg/ml IN 50 mM sodium citrate pH 6.5, 0.5 M NaCl, 5 mM magnesium cloride, 50 mM arginine hydrocloride, 50 mM Na L-glutamate. CRYSTALLIZATION SOLUTION: 0.1M Na acetate pH 4.5, 40% PEG 200 |