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 |