5NE8

Crystal structure of H307A mutant of Thermotoga maritima 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)	0.9801
Spacegroup name	P 1 21 1
Unit cell lengths	42.790, 138.650, 61.250
Unit cell angles	90.00, 110.51, 90.00

Refinement procedure

Resolution	40.107 - 1.750
R-factor	0.1686
Rwork	0.165
R-free	0.18500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p6y
RMSD bond length	0.012
RMSD bond angle	1.263
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]	40.107	40.107	1.790
High resolution limit [Å]	1.750	7.820	1.750
Rmerge	0.056	0.034	0.563
Rmeas	0.060	0.037	0.609
Number of reflections	67094	772	4879
<I/σ(I)>	17.96	43.73	2.38
Completeness [%]	99.5	98.3	97.2
Redundancy	6.732	6.911	6.786
CC(1/2)	0.999	0.997	0.841

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	292	TmPep1050 H307A (230 uM) was crystallised in 0.1 M sodium citrate 10 % PEG3350 pH4.5