1OMZ

crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) in complex with UDPGalNAc

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-04-15
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 4 21 2
Unit cell lengths	126.339, 126.339, 83.929
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.100
R-factor	0.201
Rwork	0.201
R-free	0.23300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1omx
RMSD bond length	0.006
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	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.097 *	0.396 *
Total number of observations	197735 *
Number of reflections	39701
<I/σ(I)>	17.7	2.8
Completeness [%]	98.9	95
Redundancy	5	3.2

Crystallization Conditions

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