4X8I

de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-08-11
Detector	DECTRIS PILATUS 6M
Wavelength(s)	1.71081
Spacegroup name	I 41 2 2
Unit cell lengths	203.908, 203.908, 112.443
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.062 - 2.500
R-factor	0.1802
Rwork	0.178
R-free	0.21840
Structure solution method	SAD
RMSD bond length	0.016
RMSD bond angle	1.281
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	SHELX
Refinement software	PHENIX ((phenix.refine: dev_1839))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.062	48.060	2.600
High resolution limit [Å]	2.500	9.010	2.500
Rmerge	0.192	0.129	1.248
Rpim	0.040	0.026	0.422
Total number of observations	872739	23973	32244
Number of reflections	39432
<I/σ(I)>	14.6	42.8	1.9
Completeness [%]	96.1	99.3	77.4
Redundancy	22.1	24.5	9.2
CC(1/2)	0.998	0.998	0.481

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.7	293	drop : 1.5 ul of protein+1.5 ul reservoir (HEPES 0.1 M pH 7.7, NH4CH3COO 0.2 M, 2 mM CoCl2, MPD 44%) +1.5 Gd-DO3A 300 mM