1QLR

CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF A HUMAN MONOCLONAL 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]	291
Detector technology	IMAGE PLATE
Collection date	1998-02-15
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	115.660, 115.660, 174.950
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	13.100 - 2.830
R-factor	0.216 *
Rwork	0.216
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dfb
RMSD bond length	0.014
RMSD bond angle	0.047
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	13.100	2.890
High resolution limit [Å]	2.830	2.830
Rmerge	0.069
Number of reflections	31329
Completeness [%]	96.8	99 *
Redundancy	2.8

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)