1TOL

FUSION OF N-TERMINAL DOMAIN OF THE MINOR COAT PROTEIN FROM GENE III IN PHAGE M13, AND C-TERMINAL DOMAIN OF E. COLI PROTEIN-TOLA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F2
Synchrotron site	CHESS
Beamline	F2
Temperature [K]	100
Detector technology	CCD
Collection date	1998-04-01
Detector	ADSC
Spacegroup name	P 43 21 2
Unit cell lengths	88.880, 88.880, 63.556
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.850
R-factor	0.2275
R-free	0.29300
Structure solution method	MIRAS
RMSD bond length	0.007
RMSD bond angle	0.024
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASES
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.920
High resolution limit [Å]	1.850	1.850
Rmerge	0.042	0.446
Total number of observations	190164 *
Number of reflections	22243
<I/σ(I)>	36.4	5.85
Completeness [%]	99.6	100
Redundancy	15.1	8.05

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5		PROTEIN AT CONCENTRATION 8-12 MG/ML IN 50 MM HEPES (PH=7.5) WITH ADDITION OF DTT C=2MM, WAS CRYSTALLIZED USING VAPOR DIFFUSION FROM THE SITTING OR HANGING DROP, WITH THE SOLUTION CONTAINING 25% PEG4000, 0.08M TRIS (PH=8.5), AND 0.15 M SODIUM ACETATE AS A PRECIPITANT. BEFORE SETTING THE DROPS, PROTEIN SOLUTION WAS MIXED WITH THE PRECIPITANT IN THE RATIO 1:1. CRYSTALS WERE GROWING BEST AT TEMPERATURE 15 DEGREES CELSIUS.