1DN0

STRUCTURE OF THE FAB FRAGMENT FROM A HUMAN IGM COLD AGGLUTININ

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE D03B-MX1
Synchrotron site	LNLS
Beamline	D03B-MX1
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	110.880, 110.880, 170.760
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	100.000 - 2.280
R-factor	0.18
Rwork	0.180
R-free	0.24000
RMSD bond length	0.023
RMSD bond angle	2.410
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]		2.300
High resolution limit [Å]	2.280	2.280
Number of reflections	50825
Completeness [%]	91.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	25 *	Cauerhff, A., (1998) Protein Pept.Lett., 5, 177. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	PEG8000	14 (%(w/w))
3	1	reservoir	sodium HEPES	0.1 (M)