9S6B

Aeropyrum pernix acylaminoacyl peptidase co-crystallized with meropenem.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P13 (MX1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-12-05
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.9763
Spacegroup name	P 1
Unit cell lengths	71.042, 98.283, 98.902
Unit cell angles	105.51, 103.19, 100.39

Refinement procedure

Resolution	39.220 - 2.300
R-factor	0.1974
Rwork	0.197
R-free	0.22860
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.562
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.360
High resolution limit [Å]	2.300	10.290	2.300
Rmeas	0.081	0.047	1.022
Number of reflections	105834	1171	7565
<I/σ(I)>	9.36	27.1	1.05
Completeness [%]	98.1	96.5	95
Redundancy	3
CC(1/2)	0.997	0.994	0.502

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	293	Reservoir: 0.45mM EDTA, 33mM sodium acetate buffer pH=5.0, 1.2% PEG Mw 4000; Protein solution: 0.24 mM in 20mM Tris pH=8.0, Meropenem solution: 62.5mM in methanol. Drop content: reservoir/protein/meropenem solutions= 1/1/0.5 volume ratio. Crystals were soaked in 30%w/w HbPG solurion saturated with meropenem.