2KMB

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

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-04-05
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 1 2 1
Unit cell lengths	79.100, 85.000, 98.800
Unit cell angles	90.00, 107.10, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.19
Rwork	0.190
R-free	0.24700
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	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.060	0.264
Number of reflections	41761
<I/σ(I)>	10.6	3.7
Completeness [%]	98.6	93.2
Redundancy	2.4	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.8	22 *	8-10% PEG 8000, 2% PEG 1000, 1 MM TRIS-CL, PH 7.8, 200 MM NACL, 20 MM CACL2, 2 MM NAN3. PRIOR TO DATA COLLECTION, THE CRYSTAL WAS ADAPTED TO THE MOTHER LIQUOR PLUS 20% MPD PLUS 80 MM 3'-NEUAC-LEWIS-X.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop		25 (mM)
10	1	reservoir	PEG8000	8-10 (%(w/v))
11	1	reservoir	PEG1000	2 (%)
12	1	reservoir	Tris-HCl	100 (mM)
13	1	reservoir		200 (mM)
14	1	reservoir		20 (mM)
15	1	reservoir		2 (mM)
2	1	drop		2.5 (mM)
3	1	drop	protein	1 (mg/ml)
4	1	drop	PEG8000	4-5 (%(w/v))
5	1	drop	PEG1000	1 (%)
6	1	drop	Tris-HCl	50 (mM)
7	1	drop		100 (mM)
8	1	drop		10 (mM)
9	1	drop		1 (mM)