7S77

Crystal structure of the G391V variant of human PGM-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CMOS
Collection date	2018-11-15
Detector	RDI CMOS_8M
Wavelength(s)	1.000001
Spacegroup name	P 41 21 2
Unit cell lengths	171.050, 171.050, 100.430
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.180 - 2.800
R-factor	0.1956
Rwork	0.193
R-free	0.25180
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	5epc
RMSD bond length	0.009
RMSD bond angle	1.095
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.180	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.160	2.240
Rmeas	0.160
Rpim	0.045	0.830
Number of reflections	37211	3643
<I/σ(I)>	15.44	1.24
Completeness [%]	99.5	99.95
Redundancy	13.2	13.7
CC(1/2)	0.999	0.512

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	condition 2-33 of the Morpheus crystal screen (Molecular Dimensions) at a protein concentration of 10 mg/mL from a hanging drop of 1 ml protein and 4 ml well buffer. Condition 2-33 contains 0.1 M of a carboxylic acid mixture (0.2 M sodium formate, 0.2 M ammonium acetate, 0.2 M sodium citrate tribasic dihydrate, 0.2 M sodium potassium tartrate tetrahydrate, and 0.2 M sodium oxamate), 0.1 M of a buffer system at pH 8.5 (Tris base and BICINE), and a 30% v/v precipitant mix (40% v/v PEG 500 MME and 20% w/v PEG 20000)