5IBQ
Crystal structure of an ABC solute binding protein from Rhizobium etli CFN 42 (RHE_PF00037,TARGET EFI-511357) in complex with alpha-D-apiose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-12-11 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 93.272, 36.924, 95.619 |
| Unit cell angles | 90.00, 118.02, 90.00 |
Refinement procedure
| Resolution | 30.979 - 1.200 |
| R-factor | 0.1506 |
| Rwork | 0.150 |
| R-free | 0.16400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ry0 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.969 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.2.8) |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 41.170 | 41.170 | 1.220 |
| High resolution limit [Å] | 1.200 | 6.460 | 1.200 |
| Rmerge | 0.068 | 0.025 | 0.674 |
| Rmeas | 0.079 | 0.030 | 0.789 |
| Rpim | 0.041 | 0.016 | 0.408 |
| Total number of observations | 319876 | 1936 | 15425 |
| Number of reflections | 85430 | ||
| <I/σ(I)> | 11.7 | 36.5 | 2 |
| Completeness [%] | 95.1 | 91.4 | 92 |
| Redundancy | 3.7 | 3.4 | 3.7 |
| CC(1/2) | 0.999 | 0.998 | 0.726 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | Protein (10 mM HEPES pH 7.5, 5 mM DTT, 10 mM D-apiose) incubate at 37 degrees C for 30 minutes; Reservoir (MCSG1 B6, 0.2 M Calcium Acetate, 0.1 M MES pH 6.0, 20 %(w/v) PEG 8000); Cryoprotection (20% glucose) |
