5UN8

Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	80
Detector technology	CCD
Collection date	2016-06-04
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.978
Spacegroup name	P 1 21 1
Unit cell lengths	89.909, 95.393, 149.320
Unit cell angles	90.00, 96.91, 90.00

Refinement procedure

Resolution	148.240 - 2.130
R-factor	0.1866
Rwork	0.184
R-free	0.22945
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5tke
RMSD bond length	0.020
RMSD bond angle	1.874
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0131)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	148.240	2.180
High resolution limit [Å]	2.130	2.140
Rpim	0.042	0.379
Number of reflections	139265	6934
<I/σ(I)>	18.4	2
Completeness [%]	99.9	100
Redundancy	4.9	4.5
CC(1/2)		0.781

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		293	0.032 M ammonium citrate tribasic (pH 7.0), 0.02 M MES monohydrate, 0.016 M imidazole, 0.002 M zinc sulfate heptahydrate, 0.128 M potassium thiocyanate, 12.8% w/v polyethylene glycol 3,350, 3.2% w/v polyethylene glycol monomethyl ether 2,000, and 5% w/v polyethylene glycol monomethyl ether 550.