6EBY
Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.450, 58.290, 58.700 |
| Unit cell angles | 90.00, 107.21, 90.00 |
Refinement procedure
| Resolution | 29.452 - 1.850 |
| R-factor | 0.2031 |
| Rwork | 0.200 |
| R-free | 0.23460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ea3 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.580 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 58.290 | 58.290 | 1.890 |
| High resolution limit [Å] | 1.850 | 9.060 | 1.850 |
| Rmerge | 0.072 | 0.053 | 0.226 |
| Rmeas | 0.077 | 0.057 | 0.242 |
| Rpim | 0.028 | 0.022 | 0.087 |
| Total number of observations | 180172 | ||
| Number of reflections | 23530 | 223 | 1463 |
| <I/σ(I)> | 17.9 | ||
| Completeness [%] | 98.1 | 98.3 | 96.9 |
| Redundancy | 7.7 | 6.4 | 7.7 |
| CC(1/2) | 0.997 | 0.995 | 0.980 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291.15 | PEG 3350, sodium chloride, BisTris |
