5DGX
1.73 Angstrom resolution crystal structure of the ABC-ATPase domain (residues 357-609) of lipid A transport protein (msbA) from Francisella tularensis subsp. tularensis SCHU S4 in complex with ADP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-08-24 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.597, 70.886, 46.647 |
| Unit cell angles | 90.00, 103.77, 90.00 |
Refinement procedure
| Resolution | 21.940 - 1.730 |
| R-factor | 0.19635 |
| Rwork | 0.194 |
| R-free | 0.23282 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fgk |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.614 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.760 |
| High resolution limit [Å] | 1.730 | 1.730 |
| Rmerge | 0.061 | 0.570 |
| Number of reflections | 23573 | |
| <I/σ(I)> | 20.3 | 3.1 |
| Completeness [%] | 90.4 | 97.3 |
| Redundancy | 5.1 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | protein: 8.2 mg/ml in 10 mM Tris-HCl pH 8.3 0.5 mM TCEP 10 mM ADP 10 mM MgCl2 crystallization: The Classics II F11 (71): 0.2 M NaCl 0.1 M Bis-Tris pH 6.5 25% (w/v) PEG 3350 cryo: crystallization condition |
