3U2D
S. aureus GyrB ATPase domain in complex with small molecule inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-09-04 |
| Detector | RIGAKU SATURN 944 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 143.487, 55.646, 51.103 |
| Unit cell angles | 90.00, 100.38, 90.00 |
Refinement procedure
| Resolution | 51.770 - 1.850 |
| R-factor | 0.2024 |
| Rwork | 0.201 |
| R-free | 0.23220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.939 |
| Data reduction software | d*TREK (9.8L) |
| Data scaling software | d*TREK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.770 | 51.770 | 1.920 |
| High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
| Rmerge | 0.095 | 0.051 | 0.335 |
| Total number of observations | 10718 | 8073 | |
| Number of reflections | 33210 | ||
| <I/σ(I)> | 6.6 | 16.2 | 2.2 |
| Completeness [%] | 97.6 | 97.8 | 92.4 |
| Redundancy | 3.02 | 3.08 | 2.57 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | sitting drop, inhibitor soak | 7.5 | 293 | 19-30% PEG3350, 0.1MHepes, pH 7.5, 0.2M MgCl2, sitting drop, inhibitor soak, temperature 293K |
