7MYM

Crystal structure of Escherichia coli dihydrofolate reductase in complex with TRIMETHOPRIM and NADPH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-08-21
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.9201
Spacegroup name	C 2 2 21
Unit cell lengths	65.470, 113.397, 216.578
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.760 - 3.040
R-factor	0.2181
Rwork	0.215
R-free	0.28230
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4psy
RMSD bond length	0.006
RMSD bond angle	1.474
Data reduction software	MOSFLM
Data scaling software	Aimless (0.7.4)
Phasing software	MrBUMP
Refinement software	REFMAC (7.1.001)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	56.760	3.250
High resolution limit [Å]	3.040	3.040
Rmerge	0.289	0.863
Rmeas	0.318	0.966
Rpim	0.127	0.416
Number of reflections	15680	16148
<I/σ(I)>	3.9	1.9
Completeness [%]	98.7	98.1
Redundancy	6	5.8
CC(1/2)	0.940	0.345

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277.15	18% to 20% PEG4000 or 8000, 0.2M ammonium sulfate and 2mM DTT.