6IBH

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 1 21 1
Unit cell lengths	32.940, 67.590, 68.900
Unit cell angles	90.00, 97.94, 90.00

Refinement procedure

Resolution	68.240 - 1.820
R-factor	0.1691
Rwork	0.167
R-free	0.20753
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.386
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC (5.8.0230)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	68.250	1.870
High resolution limit [Å]	1.820	1.820
Rmeas	0.097	0.911
Number of reflections	25629	1351
<I/σ(I)>	11.79
Completeness [%]	95.1	68.9
Redundancy	7.4	6.3
CC(1/2)	0.997	0.816

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	1:1 ratio of protein:reservoir solution in MRC plates using an Oryx-8 robot. Protein concentration: 13.3 mg/ml Reservoir solution (Morpheus screen #40): 12.5 (w/v)MPD, 12.5 (w/v)PEG1000, 12.5 (w/v)PEG3350. 20mM 1,6-hexanediol, 20mM 1-butanol, 20mM (RS)1,2-propandiol, 20mM 2-propanol, 20mM 1,4-butandiol, 20mM 1,3-propandiol. 50 mM MES monohydrate pH 6.5, 50 mM imidazole pH 6.5.