1RIH

Crystal Structure of Fab 14F7, a unique anti-tumor antibody specific for N-glycolyl GM3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	293
Detector technology	CCD
Collection date	2001-06-26
Detector	MARRESEARCH
Wavelength(s)	1.093
Spacegroup name	P 21 21 21
Unit cell lengths	52.500, 78.900, 121.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.500
R-factor	0.184
Rwork	0.181
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c5c
RMSD bond length	0.009
RMSD bond angle	1.600
Data reduction software	XDS
Data scaling software	XDS
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.062	0.367
Number of reflections	17766
<I/σ(I)>	13.8	3.5
Completeness [%]	97.9	97.5
Redundancy	4.2	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.8 *	293	15% PEG 400, 100 mM Hepes, (25 mM Tris), pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K
1	VAPOR DIFFUSION, HANGING DROP	8.8 *	293	15% PEG 400, 100 mM Hepes, (25 mM Tris), pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris	25 (mM)	pH8.8
3	1	reservoir	PEG400	15 (%)
4	1	reservoir	HEPES	100 (mM)	pH7.0