6NW5

Crystal structure of TmPep1050 aminopeptidase with its metal cofactors

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	2018-12-10
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.980
Spacegroup name	H 3
Unit cell lengths	131.152, 131.152, 285.610
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.602 - 1.700
R-factor	0.1436
Rwork	0.143
R-free	0.16360
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p6y
Data reduction software	XDS (20180808)
Data scaling software	XSCALE (20180808)
Phasing software	PHASER (2.8.2)
Refinement software	PHENIX (1.14-3260-00)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.602	47.602	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.082	0.030	0.670
Rmeas	0.087	0.032	0.704
Number of reflections	201316	2238	14587
<I/σ(I)>	15.81	40.12	2.81
Completeness [%]	99.8	99.5	97.6
Redundancy	10.345	10.597	10.409
CC(1/2)	0.999	1.000	0.871

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	292	TmPep1050 (1 mM in 50 mM MOPS 0.5 M ammonium sulfate 1 mM CoCl2 pH7.2) was crystallised in 0.18 M tri-ammonium citrate pH7.5 PEG3350 40%