8AVS

Racemic protein crystal structure of aureocin A53 from Staphylococcus aureus in the presence of citrate and acetate

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	2019-12-15
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9119
Spacegroup name	C 1 2 1
Unit cell lengths	73.070, 37.280, 113.950
Unit cell angles	90.00, 93.05, 90.00

Refinement procedure

Resolution	36.480 - 1.210
Rwork	0.187
R-free	0.22080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2n8o
RMSD bond length	0.010
RMSD bond angle	1.339
Data reduction software	xia2
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.480	1.230
High resolution limit [Å]	1.210	1.210
Number of reflections	90457	3651
<I/σ(I)>	8.8	1
Completeness [%]	96.6	80.3
Redundancy	3.1	1.8
CC(1/2)	0.998	0.617

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	292	A racemic mixture of L-Aureocin A53 and D-Aureocin A53 at 40 mg/mL concentration was mixed 1:1 with 0.2 M ammonium acetate, 0.2 M sodium citrate and 29% PEG 4000 v/v precipitant condition, pH 5.6 in a 1 microlitre sitting drop. Crystals were submerged in 20% PEG 400 in the precipitant solution as cryoprotectant and flash frozen in liquid nitrogen during harvesting.