8ARN
Crystal structure of the peptide binding protein, OppA, from Bacillus subtilis in complex with an endogenous tetrapeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-07-04 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.82 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.520, 65.890, 153.290 |
Unit cell angles | 90.00, 100.97, 90.00 |
Refinement procedure
Resolution | 55.025 - 1.500 |
Rwork | 0.177 |
R-free | 0.20660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rkm |
RMSD bond length | 0.010 |
RMSD bond angle | 1.614 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 55.025 | 54.960 | 1.530 |
High resolution limit [Å] | 1.500 | 8.220 | 1.500 |
Rmerge | 0.045 | 0.037 | 0.723 |
Rmeas | 0.059 | 0.049 | 0.955 |
Rpim | 0.038 | 0.031 | 0.617 |
Number of reflections | 158694 | 1028 | 7829 |
<I/σ(I)> | 12.6 | ||
Completeness [%] | 99.9 | ||
Redundancy | 4.2 | 3.7 | 4.2 |
CC(1/2) | 0.998 | 0.996 | 0.609 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | Crystals of OppA were obtained from hanging drops composed of 2 microlitres of reservoir solution consisting of 0.1 M MMT, 22.5% PEG 1500 and 2.5% DMSO pH 8.0 and 2 microlitres protein at 18 mg.ml-1 with crystal optimisation following a seeding protocol. |