6IBJ

Copper binding protein from Laetisaria arvalis (LaX325)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-20
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9799
Spacegroup name	P 43 21 2
Unit cell lengths	74.920, 74.920, 64.390
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.880 - 2.100
R-factor	0.19647
Rwork	0.194
R-free	0.25618
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6ibi
RMSD bond length	0.010
RMSD bond angle	1.255
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0230)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	2.150
High resolution limit [Å]	2.100	2.100
Rmeas	0.087	0.170
Number of reflections	11173	807
<I/σ(I)>	12.25	1.49
Completeness [%]	99.9	99.9
Redundancy	7.2	7.44
CC(1/2)	0.999	0.803

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	20 mM L-Na-Glutamate, 20 mM DL-Alanine (racemic), 20 mM Glycine, 20 mM DL-Lysine HCl (racemic), 20 mM DL-Serine (racemic) 100 mM MES monohydrate pH 6.5 / 100 mM imidazole pH 6.5 20% (w/v) PEG 500 MME and 10% (w/v) PEG 20.000.