6MA5

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2016-04-21
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9792
Spacegroup name	P 61 2 2
Unit cell lengths	98.790, 98.790, 365.910
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	55.612 - 2.000
R-factor	0.1815
Rwork	0.180
R-free	0.21040
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	4n3a
RMSD bond length	0.007
RMSD bond angle	0.730
Data reduction software	iMOSFLM (7.2.2)
Data scaling software	Aimless (0.5.12)
Phasing software	PHENIX
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	55.612	55.610	2.040
High resolution limit [Å]	2.000	9.800	2.000
Rmerge	0.119	0.037	0.976
Rmeas	0.134	0.043	1.132
Rpim	0.060	0.020	0.562
Number of reflections	72159	786	4170
<I/σ(I)>	7.1
Completeness [%]	99.4	99.1	95.2
Redundancy	4.7	4.1	3.8
CC(1/2)	0.995	0.998	0.547

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	1.05 M Sodium Citrate Tribasic Dihydrate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K