1BFV

MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-02
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 4 21 2
Unit cell lengths	89.900, 89.900, 59.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.100
R-factor	0.187 *
Rwork	0.187
R-free	0.27100
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	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.074 *
Total number of observations	129898 *
Number of reflections	14834
<I/σ(I)>	9.53	3.1
Completeness [%]	99.8	99.5
Redundancy	8.8	8.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7 *		PROTEIN WAS CRYSTALLIZED FROM 18% (W/V) PEG 8000, 200MM ZN ACETATE AND 100MM NA CACODYLATE, PH 7.5

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	zinc acetate	0.1 (M)
3	1	drop	sodium cacodylate	0.05 (M)
4	1	drop	PEG8000	9 (%(w/v))
5	1	reservoir	zinc acetate	0.2 (M)
6	1	reservoir	sodium cacodylate	0.1 (M)
7	1	reservoir	PEG8000	18 (%(w/v))