1K4V

1.53 A Crystal Structure of the Beta-Galactoside-alpha-1,3-galactosyltransferase in Complex with UDP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	0.909
Spacegroup name	P 1 21 1
Unit cell lengths	45.022, 94.145, 94.382
Unit cell angles	90.00, 98.92, 90.00

Refinement procedure

Resolution	40.000 - 1.530
R-factor	0.1405 *
Rwork	0.141
R-free	0.19060
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1g93
RMSD bond length	0.014
RMSD bond angle	2.170 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.580
High resolution limit [Å]	1.530	1.530
Rmerge	0.106 *	0.497 *
Total number of observations	386939 *
Number of reflections	114924
<I/σ(I)>	11.73	1.98
Completeness [%]	98.2	93.8
Redundancy	3.37

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6 *	16 *	PEG6000, TRIS/HCL, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop	MES/NaOH	20 (mM)	pH6.0
3	1	drop	glycerol	10 (%)
4	1	drop	UDP	10 (mM)
5	1	drop		0.1 (mM)
6	1	reservoir	PEG6000	5 (%)
7	1	reservoir	Tris-HCl	0.1 (M)	pH8.0