7O58

Human phosphomannomutase 2 (PMM2) with mutation T237M in complex with the activator glucose 1,6-bisphosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALBA BEAMLINE XALOC
Synchrotron site	ALBA
Beamline	XALOC
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-07-09
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97926
Spacegroup name	P 65 2 2
Unit cell lengths	70.520, 70.520, 359.720
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	59.950 - 1.970
R-factor	0.1851
Rwork	0.183
R-free	0.22990
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7o0c
RMSD bond length	0.014
RMSD bond angle	1.215
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	59.950	2.010
High resolution limit [Å]	1.965	1.965
Rmerge	0.174	2.220
Rpim	0.042	0.524
Number of reflections	37985	2683
<I/σ(I)>	14.7	1.8
Completeness [%]	96.4	100
Redundancy	18.3	19.2
CC(1/2)	0.999	0.751

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