9NV5

Crystal structure of phosphoglycerate mutase from Trichomonas vaginalis

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	2024-12-14
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	73.780, 92.704, 94.002
Unit cell angles	90.00, 94.09, 90.00

Refinement procedure

Resolution	19.960 - 1.950
R-factor	0.1578
Rwork	0.156
R-free	0.18650
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	1.240
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((dev_5634: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.960	1.980
High resolution limit [Å]	1.950	1.950
Rmerge	0.138	1.314
Rmeas	0.150	1.419
Rpim	0.058	0.532
Total number of observations	624081	31823
Number of reflections	91791	4522
<I/σ(I)>	11.1	1.9
Completeness [%]	99.8
Redundancy	6.8	7
CC(1/2)	0.997	0.672

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	Index F7: 25% (w/v) PEG 3350, 0.1 M BIS-TRIS 6.5, 0.25 M ammonium sulfate. TrvaA.01013.a.B1.PW39315 at 18.8 mg/mL. plate SS Clover F4 IDX F7 BK 5 pg 18, Puck: PSL-0515, Cryo: 20% (v/v) PEG 200 + 80% crystallant.