3NUH
A domain insertion in E. coli GyrB adopts a novel fold that plays a critical role in gyrase function
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-07-22 |
Detector | ADSC Q315r |
Wavelength(s) | 0.97920 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 108.062, 147.493, 138.870 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.600 - 3.103 |
R-factor | 0.238 |
Rwork | 0.234 |
R-free | 0.28200 |
Structure solution method | MR-SAD |
Starting model (for MR) | The structure was solved as a combination of MR and SAD method. The starting model used corresponds to PDB ID 1AB4. |
RMSD bond length | 0.003 |
RMSD bond angle | 0.618 |
Refinement software | PHENIX (1.5_2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.600 | 3.200 |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 20320 | |
<I/σ(I)> | 3.8 | |
Completeness [%] | 99.6 | 99.6 |
Redundancy | 5 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | hanging drop | 8 | 291 | 90 mM imidazole pH 8.0, 11% isopropanol, 18 mM magnesium chloride, 10 mM spermidine, 3% pentaerythritol ethoxylate 15/4, hanging drop, temperature 291K |