6I9Y

The 2.14 A X-ray crystal structure of Sporosarcina pasteurii urease in complex with Au(I) ions

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID30B
Synchrotron site	ESRF
Beamline	ID30B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-06-21
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.9677
Spacegroup name	P 63 2 2
Unit cell lengths	132.291, 132.291, 190.435
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	45.800 - 2.140
R-factor	0.17262
Rwork	0.171
R-free	0.20801
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5g4h
RMSD bond length	0.006
RMSD bond angle	1.091
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	REFMAC
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.800	2.200
High resolution limit [Å]	2.140	2.140
Rmerge	0.139	1.509
Rmeas	0.157	1.710
Rpim	0.070	0.785
Number of reflections	54809	4421
<I/σ(I)>	11.2	1.5
Completeness [%]	100.0	100
Redundancy	8.9	8.8
CC(1/2)	0.997	0.627

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.3	293	The protein-ligand complex in 50 mM HEPES buffer, pH 7.50 (also containing 5% (v/v) DMSO), was diluted with an equal volume of 1.5 M ammonium sulfate containing the same concentration of ligand and DMSO.