4N39

Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2011-07-19
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.075
Spacegroup name	P 32 2 1
Unit cell lengths	101.170, 101.170, 131.730
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	33.116 - 1.760
R-factor	0.1887
Rwork	0.187
R-free	0.21580
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.899
Data reduction software	iMOSFLM
Data scaling software	SCALA (3.3.16)
Phasing software	PHENIX
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	87.616	33.116	1.860
High resolution limit [Å]	1.760	5.570	1.760
Rmerge		0.044	0.628
Total number of observations		12104	58259
Number of reflections	77414
<I/σ(I)>	9.1	14	1.1
Completeness [%]	99.6	92.3	100
Redundancy	5.1	4.9	5.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	1.5 M Potassium Sodium Tartrate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K