10UH

Crystal structure of Formyl-coenzyme A transferase from Brucella melitensis in complex with CoA

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	2025-04-05
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	C 2 2 21
Unit cell lengths	95.054, 176.355, 213.183
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.680 - 1.850
R-factor	0.1754
Rwork	0.175
R-free	0.19120
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.594
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]	48.680	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.155	1.726
Rmeas	0.161	1.791
Rpim	0.044	0.476
Total number of observations	2034117	156594
Number of reflections	151962	11162
<I/σ(I)>	17.1	1.7
Completeness [%]	99.9
Redundancy	13.4	14
CC(1/2)	0.996	0.738

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	Index G7: 0.20M Ammonium Acetate, 0.1M Bis-Tris pH 6.5, 20% PEG 3350. BrmeA.18114.b.B2.PW39356 at 20.7 mg/mL. Cocrystallization with 2mM CoA. plate 19820 G7 drop 2, Puck: PSL-1916, Cryo: 20% PEG 200 + 80% crystallant