39RG

Crystal structure of a formate acetyltransferase (PFL) from Amygdalobacter indicium (CoA complex)

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	2026-08-06
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 32 2 1
Unit cell lengths	102.526, 102.526, 228.971
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	48.110 - 2.200
R-factor	0.1868
Rwork	0.184
R-free	0.23770
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.851
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (2.2.1_6174)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.110	2.190
High resolution limit [Å]	2.150	2.150
Rmerge	0.081	1.646
Rmeas	0.085	1.722
Rpim	0.025	0.503
Total number of observations		51447
Number of reflections	76636	4488
<I/σ(I)>	15.6	1.5
Completeness [%]	100.0
Redundancy	11	11.5
CC(1/2)	0.999	0.631

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	Morpheus Fusion A5 20% (v/v) PEG 500 MME; 10 % (w/v) PEG 20000; 0.05M Sodium HEPES; 0.05M MOPS (acid) pH 7.5; 0.02M 1,6-Hexanediol; 0.02M 1-Butanol 0.02M 1,2-Propanediol; 0.02M 2-Propanol; 0.02M 1,4-Butanediol; 0.02M 1,3-Propanediol; 0.02M DL-Glutamic acid monohydrate; 0.02M DL-Alanine; 0.02M Glycine; 0.02M DL-Lysine monohydrochloride; 0.02M DL-Serine, AminA.20507.a.A1.PW39584 at 25.1 mg/mL. Cocrystallization with 5mM CoA. plate 21327 A5 drop 2. puck PSL0805, Cryo: direct