6XG5

X-ray structure of Escherichia coli dihydrofolate reductase in complex with trimethoprim

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-07-12
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97919
Spacegroup name	P 32 2 1
Unit cell lengths	61.809, 61.809, 104.630
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.700 - 1.900
R-factor	0.2362
Rwork	0.236
R-free	0.26250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rx2
RMSD bond length	0.006
RMSD bond angle	1.385
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.058	1.616
Rmeas	0.063	1.803
Rpim	0.026	0.774
Number of reflections	18717	790
<I/σ(I)>	33.4	0.9
Completeness [%]	99.2	87.3
Redundancy	6.1	4.3
CC(1/2)	0.982	0.548

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	0.1 M sodium citrate tribasic dihydrate (pH 5.6), 0.15 M ammonium acetate and 17.5% or 20% PEG 4000; 10 mM NADPH, 2 mM trimethoprim was incubated with overnight at 293 K