7BFM

Structure of the M198F M298F double mutant of the Streptomyces coelicolor small laccase T1 copper site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALBA BEAMLINE XALOC
Synchrotron site	ALBA
Beamline	XALOC
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-06-22
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.97917
Spacegroup name	P 21 3
Unit cell lengths	178.638, 178.638, 178.638
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.770 - 2.000
R-factor	0.1463
Rwork	0.146
R-free	0.15810
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3cg8
Data reduction software	XDS
Data scaling software	Aimless (0.7.4)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.19-4092)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.770	29.770	2.030
High resolution limit [Å]	2.000	10.930	2.000
Rmerge	0.083	0.032	0.687
Rmeas	0.086	0.032	0.705
Rpim	0.019	0.007	0.156
Total number of observations	2518974	16129	128564
Number of reflections	128318	825	6362
<I/σ(I)>	24.6	54.8	4.7
Completeness [%]	100.0	95.2	99.8
Redundancy	19.6	19.6	20.2
CC(1/2)	0.999	1.000	0.939

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	Protein concentration was 20 mg/ml in 20 mM Tris-HCl buffer (pH 7.5). Mother liquor was made up of 40% PEG400, 200 mM Li2SO4 and 100 mM Tris-HCl (pH 8.5). The protein was mixed in 2:1 ratio with protein to mother liquor.