4N3A

Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A

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	2011-10-11
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.1
Spacegroup name	P 61 2 2
Unit cell lengths	98.929, 98.929, 367.015
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	45.858 - 1.880
R-factor	0.2015
Rwork	0.200
R-free	0.22220
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.062
Data reduction software	iMOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	PHENIX
Refinement software	PHENIX (1.7.3_928)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	85.675	45.858	1.980
High resolution limit [Å]	1.880	5.950	1.880
Rmerge		0.053	0.599
Total number of observations		22853	46145
Number of reflections	82602
<I/σ(I)>	7.3	12.2	1.1
Completeness [%]	95.0	93.6	96.1
Redundancy	3.8	7.9	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	0.72M Potassium Phosphate Monobasic, 0.88M Potassium Phosphate Dibasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K