3KMB

COMPLEX OF 3'-SULFO-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-06-02
Detector	MAR scanner 300 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	79.100, 84.900, 97.200
Unit cell angles	90.00, 106.60, 90.00

Refinement procedure

Resolution	10.000 - 1.950
R-factor	0.205 *
Rwork	0.204
R-free	0.25500 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rtm
RMSD bond length	0.007
RMSD bond angle	21.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.54)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.020
High resolution limit [Å]	2.000	1.950
Rmerge	0.054	0.250
Number of reflections	44240
<I/σ(I)>	11.1	4.6
Completeness [%]	98.1	95.6
Redundancy	2.5	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.8	22 *	PROTEIN WAS CRYSTALLIZED FROM 8-10% PEG 8000, 2% PEG 1000, 100 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTED, THE CRYSTAL WAS SOAKED IN THE MOTHER LIQUOR MINUS PEG 8000, PLUS 35% PEG 400, PLUS 80 MM 3'-SULFO- LEWIS-X.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2 (mg/ml)
10	1	drop	solution A
2	1	drop		50 (mM)
3	1	drop		5 (mM)
4	1	reservoir	PEG8000	8-10 (%(w/v))	solution A
5	1	reservoir	PEG1000	2 (%)	solution A
6	1	reservoir	Tris-HCl	100 (mM)	solution A
7	1	reservoirr		200 (mM)	solution A
8	1	reservoir		2 (mM)	solution A
9	1	reservoir		20 (mM)	solution A