8TBA

Crystal structure of Helicobacter pylori glutamate racemase bound to D-glutamate and a crystallographic artifact

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-11-26
Detector	DECTRIS EIGER X 16M
Wavelength(s)	.9792
Spacegroup name	P 21 21 21
Unit cell lengths	63.350, 79.868, 114.887
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	65.580 - 1.650
R-factor	0.1883
Rwork	0.187
R-free	0.21310
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.865
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	79.870	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.050	1.049
Rmeas	0.053	1.103
Rpim	0.017	0.335
Total number of observations	708160	35758
Number of reflections	70675	3437
<I/σ(I)>	21.7	2.2
Completeness [%]	99.8
Redundancy	10	10.4
CC(1/2)	0.999	0.871

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	293	10g/l Glutamate Racemase in crystal buffer (0.2M Ammonium Acetate, 5mM D/L-glutamate, 1mM TCEP, pH 7.4) with 10% DMSO and 2.5mM compound (incubated in fridge for 1 week) combined 2:1 with INDEX G4 (25% PEG3350, 0.2M LiSO4, 0.1M Tris Base) pH 7.6