1OMX

Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-03-05
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 4 21 2
Unit cell lengths	125.903, 125.903, 83.068
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.400
R-factor	0.203
Rwork	0.203
R-free	0.24000
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	23.700 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.400
Rmerge	0.073 *	0.280 *
Total number of observations	127306 *
Number of reflections	26171
<I/σ(I)>	14.9
Completeness [%]	98.3	86.8 *
Redundancy	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	10-12% PEG3000, 200mM MgCl2, 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)