7EP9

The structure of carboxypeptidase from Fusobacterium nucleatum

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-11-20
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97934
Spacegroup name	P 21 21 2
Unit cell lengths	192.004, 124.797, 128.898
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.830 - 2.604
R-factor	0.2317
Rwork	0.229
R-free	0.27380
Structure solution method	SAD
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	PHENIX (1.14_3228)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.690
High resolution limit [Å]	2.600	2.600
Rmerge		0.700
Number of reflections	95180	94966
<I/σ(I)>	10.2
Completeness [%]	100.0
Redundancy	12.7
CC(1/2)	0.840

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289.15	21%PEG_2000 and 0.1 M Tris pH 7.9