1FD9

CRYSTAL STRUCTURE OF THE MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN (MIP) A MAJOR VIRULENCE FACTOR FROM LEGIONELLA PNEUMOPHILA

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-12-02
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	80.750, 80.750, 103.260
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.400 - 2.410
R-factor	0.2302
Rwork	0.230
R-free	0.28050 *
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	22.100 *
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.400	2.550
High resolution limit [Å]	2.410	2.600 *
Rmerge	0.103 *	0.428 *
Total number of observations	52836 *
Number of reflections	10976 *
<I/σ(I)>	2.7	2.4
Completeness [%]	99.4 *	99.7 *
Redundancy	4.8 *	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5	288	PEG 8,000, zinc acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MES	100 (mM)	pH6.1-6.5
2	1	reservoir	PEG8000	15-20 (%(w/v))
3	1	reservoir	zinc acetate	500 (mM)
4	1	drop	protein	10 (mg/ml)
5	1	drop	HEPES	20 (mM)	pH7.0