9O57

Crystal structure of Thymidylate kinase (Tmk) from Klebsiella aerogenes.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2025-02-15
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 21 21 21
Unit cell lengths	66.407, 75.450, 76.018
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.460 - 2.850
R-factor	0.2396
Rwork	0.238
R-free	0.26790
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.664
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (dev_5660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.460	3.000
High resolution limit [Å]	2.850	2.850
Rmerge	0.158	1.281
Rmeas	0.168	1.364
Rpim	0.056	0.460
Total number of observations	79766	11261
Number of reflections	9361	1348
<I/σ(I)>	10.1	1.6
Completeness [%]	99.7
Redundancy	8.5	8.4
CC(1/2)	0.998	0.699

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	291	PACT B2: 0.10 M MIB buffer, pH 5.0, 25% PEG 1500. KlaeA.01628.a.B1.PW39187 at 19.7 mg/mL. plate 19509 well B2 drop 2, 2mM UMP added to the protein prior to crystallization but ligand is not bound. Puck: PSL-0313, Cryo: 0.10M MIB buffer, pH 5.0, 35% PEG 1500.