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.