7K62

Crystal Structure of Dihydrofolate reductase from Mycobacterium kansasii in complex with NADP and inhibitor P218

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-08-06
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	62.100, 66.250, 86.120
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.390 - 2.050
R-factor	0.216
Rwork	0.211
R-free	0.26830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1df7 as per Morda
RMSD bond length	0.007
RMSD bond angle	0.919
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.18.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.100
High resolution limit [Å]	2.050	9.170	2.050
Rmerge	0.060	0.021	0.598
Rmeas	0.067	0.024	0.692
Number of reflections	22844	296	1637
<I/σ(I)>	14.45	44.62	1.99
Completeness [%]	99.7	97	99.3
Redundancy	5.108	4.361	3.947
CC(1/2)	0.999	0.999	0.826

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	287	Microlytics Morpheus screen, condition E4: 12.5% (w/V) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (V/V) MPD: 30mM of each diethyleneglycol, triethyleneglycol, tetraethyleneglycol, pentaethyleneglycol: 100mM MES/imidazole pH 6.5. MykaA.01062.a.B1.PS38569 at 5.22mg/ml + 2mM each NADP and P218: tray 309622 e4: cryo: direct: puck kdu7-7