2BFV

MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-04
Detector	RIGAKU
Spacegroup name	P 32
Unit cell lengths	53.600, 53.600, 83.800
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.500
R-factor	0.176 *
Rwork	0.187
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nbv
RMSD bond length	0.011
RMSD bond angle	0.037
Data reduction software	MOSFLM
Data scaling software	CCP4 ((ROTAVATA))
Phasing software	AMoRE
Refinement software	PROLSQ

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.064 *	0.225 *
Total number of observations	12233 *
Number of reflections	7836
<I/σ(I)>	7.21	2.6
Completeness [%]	86.9	87.5
Redundancy	1.5	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5		PROTEIN WAS CRYSTALLIZED FROM 15% (W/V) PEG 4000, 100MM NA ACETATE AND 50MM TRIS HCL PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.5-3 (mg/ml)
2	1	drop	Na acetate	0.05 (M)
3	1	drop	Tris-HCl	0.025 (M)
4	1	drop	PEG4000	7.5 (%(w/v))
5	1	reservoir	Na acetate	0.1 (M)
6	1	reservoir	Tris-HCl	0.05 (M)
7	1	reservoir	PEG4000	15 (%(w/v))