9VWU

Crystal structure of AetF-V220I in complex with FAD and L-tryptophan

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSRRC BEAMLINE TPS 07A
Synchrotron site	NSRRC
Beamline	TPS 07A
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-07-20
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.97621
Spacegroup name	P 21 21 21
Unit cell lengths	59.665, 75.207, 143.828
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.510 - 1.910
R-factor	0.18797
Rwork	0.185
R-free	0.24080
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.498
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	25.000	25.000	1.980
High resolution limit [Å]	1.910	4.110	1.910
Rmerge	0.053	0.035	0.596
Rmeas	0.062	0.041	0.675
Rpim	0.029	0.021	0.308
Total number of observations	214536
Number of reflections	49176	4921	4872
<I/σ(I)>	10
Completeness [%]	97.4	92.1	98.3
Redundancy	4.4	3.8	4.3
CC(1/2)	0.994	0.997	0.892

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	30% PEG 6000, 100 mM Tris pH 8.0, 10 mg/mL AetF-V220I (2 mM Trp, 5 mM DTT)