8AZB

Crystal Structure of the peptide binding protein DppE from Bacillus subtilis in the unliganded state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I02
Synchrotron site	Diamond
Beamline	I02
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-02-01
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97949
Spacegroup name	P 21 21 21
Unit cell lengths	54.530, 91.080, 106.740
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.089 - 1.400
Rwork	0.181
R-free	0.20840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	8ay0
RMSD bond length	0.012
RMSD bond angle	1.810
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]	46.090	46.050	1.420
High resolution limit [Å]	1.400	7.670	1.400
Rmerge	0.046	0.034	0.344
Rmeas	0.053	0.039	0.436
Rpim	0.026	0.020	0.262
Number of reflections	104801	734	5040
<I/σ(I)>	20.9
Completeness [%]	99.6
Redundancy	7.4	6.6	4.4
CC(1/2)	0.999	0.996	0.886

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	Ligand free DppE was crystallised in a sitting drop formed by mixing 150 nl of the unliganded protein at 9 mg.ml-1 with 150 nl of 0.1 M MIB buffer pH 4.0, 25 % (w/v) PEG 1500.