1ON6

Crystal structure of mouse alpha-1,4-N-acetylhexosaminotransferase (EXTL2) in complex with UDPGlcNAc

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-03-26
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 4 21 2
Unit cell lengths	126.064, 126.064, 83.936
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.300
R-factor	0.196
Rwork	0.196
R-free	0.23400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Apo enzyme pdb:1OMX
RMSD bond length	0.006
RMSD bond angle	24.000 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.064 *	0.299 *
Total number of observations	248026 *
Number of reflections	27856
<I/σ(I)>	23.2	3.3
Completeness [%]	91.1	72.9
Redundancy	8.9	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	PEG3000, mgcl2, cacodyltate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	25 (mM)	pH7.5
2	1	drop		100 (mM)
3	1	reservoir	sodium cacodylate	0.1 (M)	pH7.5
4	1	reservoir	PEG3000	10-12 (%)
5	1	reservoir		200 (mM)