11EG

Crystal Structure of L-erythrulose-1-phosphate isomerase from Brucella melitensis (P1 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
Unit cell lengths	45.259, 49.359, 116.827
Unit cell angles	88.41, 83.15, 86.23

Refinement procedure

Resolution	49.240 - 1.600
R-factor	0.1568
Rwork	0.155
R-free	0.18280
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.736
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]	49.240	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.084	0.660
Rmeas	0.099	0.795
Rpim	0.052	0.435
Total number of observations	449107	25173
Number of reflections	125292	7690
<I/σ(I)>	9.5	1.6
Completeness [%]	94.8
Redundancy	3.6	3.3
CC(1/2)	0.997	0.652

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Berkeley B2: 100 mM HEPES, pH 7.5, 400 mM NaCl, 30% PEG 3350. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. plate 20692 B2 drop 1, Puck: PSL-2008, Cryo: Berkeley B2.