7O1B

Human phosphomannomutase 2 (PMM2) wild-type co-crystallized with the activator glucose 1,6-bisphosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-03-11
Detector	DECTRIS PILATUS 2M
Wavelength(s)	0.966
Spacegroup name	P 65 2 2
Unit cell lengths	70.960, 70.960, 364.280
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	61.450 - 3.080
R-factor	0.2369
Rwork	0.236
R-free	0.25650
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7o0c
RMSD bond length	0.009
RMSD bond angle	1.123
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	61.450	3.129
High resolution limit [Å]	3.080	3.080
Rmerge	0.341	1.539
Rmeas	0.350
Rpim	0.081	0.364
Number of reflections	10988	514
<I/σ(I)>	8.4	2.2
Completeness [%]	99.9	100
Redundancy	18.5	18.6
CC(1/2)	0.997	0.784

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	Drops made by mixing 1 microliter of protein solution and 1 microliter of crystallization deposit solution. Protein solution contained 5 mg/ml protein and 3 mM glucose 1,6-bisphophate in 20 mM Hepes pH 7.5 and 0.2 M NaCl. Crystallization solution contained 0.3-0.4 M MgCl2, 24% PEG3350 and 0.1 M HEPES pH 7.5