5NE6

Crystal structure of dimeric TmPep1050 aminopeptidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 2
Synchrotron site	SOLEIL
Beamline	PROXIMA 2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-11-25
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.9800
Spacegroup name	C 2 2 21
Unit cell lengths	42.550, 114.710, 267.690
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.248 - 2.000
R-factor	0.1676
Rwork	0.166
R-free	0.20320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p6y
RMSD bond length	0.004
RMSD bond angle	0.647
Data reduction software	XDS (20160617)
Data scaling software	XSCALE (20160617)
Phasing software	PHASER (2.6.0)
Refinement software	PHENIX (1.10.1-2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.248	48.248	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.095	0.050	0.691
Rmeas	0.099	0.052	0.719
Number of reflections	45086	584	3290
<I/σ(I)>	16.9	38.71	3.46
Completeness [%]	99.9	98.8	99.2
Redundancy	13.228	11.781	13.052
CC(1/2)	0.998	0.996	0.879

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	292	Dimeric TmPep1050 (230 uM in 50 mM MOPS 0.5 M ammonium sulfate pH7.2) was crystallised in 0.1 M sodium citrate 10% PEG3350 pH6.0