1G93

CRYSTAL STRUCTURE OF THE BOVINE CATALYTIC DOMAIN OF ALPHA-1,3-GALACTOSYLTRANSFERASE IN THE PRESENCE OF UDP-GALACTOSE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	2000-10-10
Detector	CUSTOM-MADE
Wavelength(s)	0.9324
Spacegroup name	P 41 21 2
Unit cell lengths	95.608, 95.608, 110.725
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.500
R-factor	0.224
Rwork	0.224
R-free	0.27200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	native crystal structure
RMSD bond length	0.015
RMSD bond angle	1.800
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.660
High resolution limit [Å]	2.500	2.500
Rmerge	0.043	0.227
Total number of observations	452447 *
Number of reflections	18010
<I/σ(I)>	9.3	2.4
Completeness [%]	99.5 *	99.5 *
Redundancy	6.7	6.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	20 *	1.3 to 1.6 M Sodium Acetate, 10 mM MnCl2, 10 mM Hg-UDP-galactgose, 500 mM NaCl, 100 mM cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-20 (mg/ml)
2	1	drop	Tris	20 (mM)
3	1	drop		2 (mM)
4	1	drop	UMP	10 (mM)
5	1	drop		500 (mM)
6	1	reservoir	sodium acetate	1.3-1.6 (M)
7	1	reservoir	cacodylate	50 (mM)