1QOO

lectin UEA-II complexed with NAG

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	104.480, 104.480, 175.350
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.750
R-factor	0.175 *
Rwork	0.174
R-free	0.20600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	UNLIGANDED UEA-II (1QNW)
RMSD bond length	0.008
RMSD bond angle	26.906 *
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]	20.000	2.840
High resolution limit [Å]	2.750	2.750
Rmerge	0.204	0.518
Total number of observations	162577 *
Number of reflections	29125	2223 *
<I/σ(I)>	10.64	3.6
Completeness [%]	99.2	97.5
Redundancy	5.42	4.96

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))