8ARE

Crystal structure of the peptide binding protein, OppA, from Bacillus subtilis in complex with a PhrE-derived pentapeptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04-1
Synchrotron site	Diamond
Beamline	I04-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-15
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.91587
Spacegroup name	I 1 2 1
Unit cell lengths	83.861, 63.689, 100.060
Unit cell angles	90.00, 114.35, 90.00

Refinement procedure

Resolution	52.263 - 1.900
Rwork	0.252
R-free	0.30840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	OppA-SNSS
RMSD bond length	0.007
RMSD bond angle	1.391
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	52.263	52.210	1.940
High resolution limit [Å]	1.900	9.110	1.900
Rmerge	0.233	0.106	1.056
Rmeas	0.313	0.140	1.415
Rpim	0.206	0.090	0.933
Number of reflections	37997	1580	9854
<I/σ(I)>	3.2
Completeness [%]	100.0
Redundancy	4.1	4.3	4
CC(1/2)	0.955	0.983	0.758

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	291	Crystals of BsOppA in complex with Ser-Arg-Asn-Val-Thr where grown from the products of an isothermal titration calorimetry experiment. This recovered material was fed into a crystallisation screening experiment in MRC-Wilden 96 well plates. A single crystal of BsOppA-SRNVT was grown from 0.1 M SPG (succinic acid, sodium dihydrogen phosphate, glycine) 25% (w/v) PEG 1500 pH 4.0,