4N3B

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-11-01
Detector	PSI PILATUS 6M
Wavelength(s)	1.1
Spacegroup name	P 61 2 2
Unit cell lengths	98.910, 98.910, 364.931
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.592 - 2.170
R-factor	0.1937
Rwork	0.192
R-free	0.22280
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.730
Data reduction software	iMOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	PHENIX
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	85.658	52.133	2.290
High resolution limit [Å]	2.170	6.880	2.170
Rmerge		0.063	0.762
Total number of observations		15024	37832
Number of reflections	56847
<I/σ(I)>	11.5	8.2	1
Completeness [%]	99.9	99.8	99.5
Redundancy	7.6	7.1	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	1.4M Sodium Malonate, 0.1M Bis Tris Propane, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K