1G1R

Crystal structure of P-selectin lectin/EGF domains complexed with SLeX

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-01-01
Detector	RIGAKU RAXIS II
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	81.140, 60.520, 91.440
Unit cell angles	90.00, 103.28, 90.00

Refinement procedure

Resolution	14.000 - 3.400
R-factor	0.227
Rwork	0.227
R-free	0.32200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.530
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.000	3.460
High resolution limit [Å]	3.400	3.400
Rmerge	0.072	0.322
Total number of observations	44334 *
Number of reflections	11667
<I/σ(I)>	29
Completeness [%]	97.8	100
Redundancy	3.79	3.79

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8.5	18 *	Tris-HCl, NaCl, CaCl2, 2-methyl-2,4-pentanediol, PEG 6000, pH 8.5, VAPOR DIFFUSION, HANGING DROP at 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	100 (mM)
3	1	drop		150 (mM)
4	1	drop		12 (mM)
5	1	drop	MPD	10 (%(v/v))
6	1	drop	PEG6000	10 (%(w/v))