5MRV

Crystal structure of human carboxypeptidase O in complex with NvCI

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	2015-10-15
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.9792
Spacegroup name	C 1 2 1
Unit cell lengths	150.114, 72.144, 90.187
Unit cell angles	90.00, 94.66, 90.00

Refinement procedure

Resolution	59.947 - 1.854
R-factor	0.1857
Rwork	0.185
R-free	0.20820
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pcu
RMSD bond length	0.011
RMSD bond angle	0.960
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	64.984	1.860
High resolution limit [Å]	1.854	1.854
Rmerge	0.069	0.800
Number of reflections	79948
<I/σ(I)>	13.9	2
Completeness [%]	98.0	96.7
Redundancy	3.5	3.4
CC(1/2)	0.998	0.680

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	291.15	Drops were prepared by mixing equal volumes of protein solution (CPO:NvCI molar ratio, 1:0.5) at 5 mg/ml (in 5 mM Tris-HCl pH 7.3, 100 mM NaCl, 1 mM B-mercaptoetanol) and reservoir solution containning HEPES pH 7.0, 200 mM ammonium choride and 20% PEG6000.