1EHH

CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI COMPLEX WITH TRI-N-ACETYLCHITOTRIOSE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	286
Detector technology	DIFFRACTOMETER
Collection date	1999-06-14
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 1 21 1
Unit cell lengths	25.550, 56.790, 55.300
Unit cell angles	90.00, 92.68, 90.00

Refinement procedure

Resolution	8.000 - 1.900
R-factor	0.183 *
Rwork	0.183
R-free	0.25300
RMSD bond length	0.014
RMSD bond angle	3.180
Data reduction software	MERGEF
Data scaling software	MERGEF
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.910	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.088	0.362
Total number of observations	44173 *
Number of reflections	13723
<I/σ(I)>	14.7
Completeness [%]	93.1	33.5
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	298	PEG1000, sodium citrate, tri-N-acetylchitotriose, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG1000	15 (%(w/v))
2	1	reservoir	citrate	0.1 (M)
3	1	drop	protein