8TQN
Crystal Structure of a MES bound Substrate Binding Protein (IseP) from an Isethionate TRAP Transporter
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-11-08 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.95372 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.669, 73.232, 95.455 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.773 - 1.650 |
Rwork | 0.197 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.524 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.773 | 47.730 | 1.680 |
High resolution limit [Å] | 1.650 | 9.040 | 1.650 |
Rmerge | 0.087 | 0.062 | 1.654 |
Rmeas | 0.092 | 0.065 | 1.790 |
Rpim | 0.028 | 0.020 | 0.671 |
Number of reflections | 37696 | 288 | 1862 |
<I/σ(I)> | 15.9 | ||
Completeness [%] | 100.0 | ||
Redundancy | 19.1 | 15.9 | 13 |
CC(1/2) | 0.999 | 0.998 | 0.764 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.2 M Lithium chloride, 0.1 M MES 6.0, 20 % w/v PEG 6000 |