11EF

Crystal Structure of L-erythrulose-1-phosphate isomerase from Brucella melitensis (P21 form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2026-01-31
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	49.668, 141.818, 94.580
Unit cell angles	90.00, 96.42, 90.00

Refinement procedure

Resolution	46.610 - 2.150
R-factor	0.1813
Rwork	0.179
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.711
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((2.0_5936: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.360	2.210
High resolution limit [Å]	2.150	2.150
Rmerge	0.168	1.292
Rmeas	0.181	1.393
Rpim	0.068	0.518
Total number of observations	492483	36696
Number of reflections	70493	5147
<I/σ(I)>	9.2	1.6
Completeness [%]	100.0
Redundancy	7	7.1
CC(1/2)	0.996	0.775

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	JCSG+ D12: 40 mM potassium phosphate, 16% PEG 8000, 20% glycerol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. plate 20694 D12 drop 1, Puck: PSL-1811, Cryo: JCSG+ D12.