4N3C

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

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	2013-02-19
Detector	PSI PILATUS 6M
Wavelength(s)	1.1
Spacegroup name	P 61 2 2
Unit cell lengths	98.880, 98.880, 365.930
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	62.517 - 2.550
R-factor	0.1858
Rwork	0.184
R-free	0.22610
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.749
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]	85.633	70.086	2.690
High resolution limit [Å]	2.550	8.060	2.550
Rmerge		0.064	0.807
Total number of observations		3333	14375
Number of reflections	33955
<I/σ(I)>	6	6.5	0.8
Completeness [%]	96.1	94.4	92.7
Redundancy	3	2.7	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.8	298	0.86M Potassium Phosphate Dibasic, 0.86M Sodium Phosphate Monobasic, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K