7RIS

Crystal structure of RPA3624, a beta-propeller lactonase from Rhodopseudomonas palustris, with active-site bound phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-11-02
Detector	DECTRIS EIGER X 9M
Wavelength(s)	1.033290
Spacegroup name	P 32 2 1
Unit cell lengths	44.540, 44.540, 189.950
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.740 - 1.720
R-factor	0.1807
Rwork	0.179
R-free	0.20110
Structure solution method	SAD
RMSD bond length	0.004
RMSD bond angle	0.705
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.740	1.782
High resolution limit [Å]	1.720	1.720
Rmerge	0.087	1.478
Rmeas	0.089	1.511
Rpim	0.020	0.330
Number of reflections	24269	2381
<I/σ(I)>	20.07	1.72
Completeness [%]	99.6	99.29
Redundancy	19.7	20.5
CC(1/2)	1.000	0.916

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Crystals were grown in a MRC SD2 microplate, set with a TTP Labtech Mosquito crystallization robot. In the crystallization experiment leading to the crystal used for data collection, 200 nL of protein solution at 10.5 mg/mL was combined with 250 nL reservoir solution, composed of 20% PEG3350, 0.2M CaCl2, 0.1M bistris buffer pH 6.5. Crystals were cryopreserved by soaking in reservoir solution supplemented to 30% PEG3350 and immersion in liquid nitrogen