9MIT

Crystal structure of Purine nucleoside phosphorylase from Trichomonas vaginalis (Hepes bound)

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	2024-10-24
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	C 1 2 1
Unit cell lengths	169.816, 49.713, 175.122
Unit cell angles	90.00, 99.18, 90.00

Refinement procedure

Resolution	46.490 - 1.490
R-factor	0.1476
Rwork	0.147
R-free	0.16780
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.972
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (dev_5533)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	172.880	1.530
High resolution limit [Å]	1.490	1.490
Rmerge	0.071	0.923
Rmeas	0.077	0.994
Rpim	0.029	0.366
Total number of observations	1617235	122232
Number of reflections	234261	17047
<I/σ(I)>	13.9	1.7
Completeness [%]	99.2
Redundancy	6.9	7.2
CC(1/2)	0.999	0.827

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Index D8: 0.1M HEPES pH 7.5, 25% PEG 3350. TrvaA.01033.d.B1.PW39308 at 17.4 mg/mL. Hepes acquired from the buffer in 3 of the subunits. plate 14433 well D8 drop 1 , Puck: PSL0911, Cryo: 80% crystallant + 20% glycerol.