6F5K

Crystal structure of laccase from Myceliophthora thermophila

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-04-06
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.966
Spacegroup name	C 2 2 21
Unit cell lengths	67.449, 128.426, 163.624
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.230 - 1.620
R-factor	0.1521
Rwork	0.150
R-free	0.18860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2q9o
RMSD bond length	0.021
RMSD bond angle	2.085
Data reduction software	XDS
Data scaling software	SCALA (0.5.24)
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.230	48.230	1.680
High resolution limit [Å]	1.620	6.270	1.620
Rmerge	0.109	0.054	0.866
Rmeas	0.123	0.061	0.971
Rpim	0.055	0.028	0.431
Number of reflections	89938	1703	8718
<I/σ(I)>	7.6	19.3	1.6
Completeness [%]	99.6	99.3	99.6
Redundancy	4.9	4.7	5
CC(1/2)	0.995	0.994	0.688

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	3 ul protein (66 mg/ml) + 2 ul reservoir solution (0.1 M HEPES pH 7.5, 34 % PEG 400, 0.22 M CaCl2, 0.05 M glycine)