1G8O

CRYSTALLOGRAPHIC STRUCTURE OF THE NATIVE BOVINE ALPHA-1,3-GALACTOSYLTRANSFERASE CATALYTIC DOMAIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-17
Detector	CUSTOM-MADE
Wavelength(s)	0.9324
Spacegroup name	P 41 21 2
Unit cell lengths	95.558, 95.558, 112.711
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 * - 2.300
R-factor	0.21 *
Rwork	0.274
R-free	0.25000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Model MAD solved at 2.8 Angstroms resolution 1fg5.pdb
RMSD bond length	0.016
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]	29.000	2.390
High resolution limit [Å]	2.300	2.300
Rmerge	0.058	0.383 *
Total number of observations	434477 *
Number of reflections	31286 *
<I/σ(I)>	8	7.8
Completeness [%]	96.5 *	96 *
Redundancy	6.9	3.7

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 UMP, 2 mM MnCl2, 500 mM NaCl, 0.1 M cacodylate, pH 6.50, 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)