7K6C

Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium abscessus ATCC 19977 / DSM 44196 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 1 21 1
Unit cell lengths	75.630, 62.490, 124.550
Unit cell angles	90.00, 94.67, 90.00

Refinement procedure

Resolution	37.690 - 2.000
R-factor	0.1666
Rwork	0.166
R-free	0.20720
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2w3v as per MORDA
RMSD bond length	0.007
RMSD bond angle	0.931
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]	37.690	37.690	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.072	0.023	0.545
Rmeas	0.084	0.027	0.653
Total number of observations	292968
Number of reflections	78407	917	5718
<I/σ(I)>	13.87	43.7	2.24
Completeness [%]	99.7	97.1	99.3
Redundancy	3.737	3.45	3.283
CC(1/2)	0.998	0.999	0.760

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	287	Optimization screen based on Microlytics MCSG1 B6: 200mM CaOAc2, 20% (w/V) PEG 8000, 100mM MES / NaOH pH 6.5: MyabA.01062.a.B15.PS38597 at 12.39mg/ml + 3.5mM NADP + 3mM P218: tray 317391 F7: cryo 20% EG + compounds: puck kdu7-5