9YFB

Crystal Structure UTP--glucose-1-phosphate uridylyltransferase from Bordetella pertussis in complex with UTP

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	2025-06-07
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 42 21 2
Unit cell lengths	73.672, 73.672, 118.422
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.680 - 1.820
R-factor	0.2003
Rwork	0.199
R-free	0.23190
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.123
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((2.0_5819: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.680	1.860
High resolution limit [Å]	1.820	1.820
Rmerge	0.055	2.175
Rmeas	0.056	2.216
Rpim	0.011	0.421
Total number of observations	776827	47984
Number of reflections	30047	1754
<I/σ(I)>	32.8	1.8
Completeness [%]	100.0
Redundancy	25.9	27.4
CC(1/2)	1.000	0.771

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291	Berkeley B9: 100mM Bis-Tris/HCL pH 6.5, 200mM Magnesium chloride, 25% PEG 3550. BopeA.00118.a.B2.PW39372 at 25.3 mg/mL. 2mM UTP + 2mM MgCl2 added to protein prior to crystallization. plate 19925 B9 drop 1, Puck: PSL-0706, Cryo: 80% crystallant + 20% glycerol