1QOT

lectin UEA-II complexed with fucosyllactose and fucosylgalactose

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]	287
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 32 2 1
Unit cell lengths	104.770, 104.770, 175.190
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 3.000
R-factor	0.192
Rwork	0.192
R-free	0.21500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UEA-II COMPLEXED WITH NAG (1QOO)
RMSD bond length	0.008
RMSD bond angle	27.770 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.140
High resolution limit [Å]	3.000	3.000
Rmerge	0.204	0.545
Total number of observations	115280 *
Number of reflections	22709	2214 *
<I/σ(I)>	8.3	3.23
Completeness [%]	98.9	98.7
Redundancy	5.08	5.11

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		Dao-Thi M.H., (1998) Acta Crystallog. sect., D54, 844. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.0-5.0 (mg/ml)
2	1	reservoir	cacodylate	100 (mM)	or MES
3	1	reservoir	PEG6000	8-16 (%(w/v))