8TA0

Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in complex with NADP and inhibitor MAM881

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SEALED TUBE
Source details	BRUKER D8 QUEST
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-06-20
Detector	Bruker PHOTON III
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	28.631, 66.290, 44.030
Unit cell angles	90.00, 91.29, 90.00

Refinement procedure

Resolution	28.620 - 1.950
R-factor	0.1549
Rwork	0.152
R-free	0.20920
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.125
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.21rc1_4933)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.020	2.000
High resolution limit [Å]	1.950	1.950
Rmerge	0.122	0.710
Rmeas	0.132	0.828
Rpim	0.050	0.418
Total number of observations	82492	3300
Number of reflections	12079	858
<I/σ(I)>	12.4	2.1
Completeness [%]	100.0
Redundancy	6.8	3.8
CC(1/2)	0.995	0.649

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	Morpheus H4: 12.5%(v/v) MPD, 12.5%(v/v) PEG 1000, 12.5%(w/v) PEG 3350, 100 mM Imidazole/MES, pH 6.5, 20 mM DL-Glutamic acid, 20 mM DL-Alanine; 20 mM Glycine, 20 mM DL-Lysine monohydrochloride and 20 mM DL-Serine. MyulA.01062.a.B13.PS38720 at 8.9 mg/mL. 2mM MAM881 and 2mM NADP added to the protein prior to crystallization. Plate 13387 well H4 drop 3, Cryo: direct