1ON8

Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) with UDP and GlcUAb(1-3)Galb(1-O)-naphthalenelmethanol an acceptor substrate analog

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-03-16
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 4 21 2
Unit cell lengths	125.157, 125.157, 83.692
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.700
R-factor	0.192
Rwork	0.192
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	pdb code: 1OMX
RMSD bond length	0.007
RMSD bond angle	23.900 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.095 *	0.393 *
Total number of observations	112343 *
Number of reflections	18492
<I/σ(I)>	11.6	4
Completeness [%]	98.6	99.6
Redundancy	6	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	PEG3000, MgCl2, cacodylate, 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)