7B2K

Structure of the M298F mutant of the Streptomyces coelicolor small laccase T1 copper axial ligand.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	100
Detector technology	CCD
Collection date	2018-04-18
Detector	ADSC QUANTUM 270
Wavelength(s)	0.97820
Spacegroup name	P 21 3
Unit cell lengths	177.620, 177.620, 177.620
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.200 - 2.200
R-factor	0.1716
Rwork	0.171
R-free	0.18510
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3cg8
Data reduction software	XDS (VERSION Jan 26, 2018)
Data scaling software	XSCALE (VERSION Jan 26, 2018)
Phasing software	PHASER (2.8.2)
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.200	29.200	2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.085	0.044	0.805
Rmeas	0.090	0.047	0.907
Total number of observations	808727
Number of reflections	92609	1100	5982
<I/σ(I)>	16.5	39.55	1.69
Completeness [%]	98.1	95.2	86.3
Redundancy	8.733	8.583	4.309
CC(1/2)	0.999	0.998	0.652

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	Protein concentration was 20 mg/mL in 20 mM Tris-HCl buffer (pH 7.5). Mother liquor was made up of 40% MPD, 200 mM NH4-OAc and 100 mM HEPES (pH 7.5). The protein was mixed in 2:1 ratio with protein to mother liquor.