1FI1

FhuA in complex with lipopolysaccharide and rifamycin CGP4832

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1999-07-03
Detector	MARRESEARCH
Spacegroup name	P 61
Unit cell lengths	172.820, 172.820, 87.910
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.900
R-factor	0.233
Rwork	0.233
R-free	0.27500
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	XDS
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.080
High resolution limit [Å]	2.900	2.900
Rmerge	0.072	0.246
Total number of observations	161168 *
Number of reflections	33363
<I/σ(I)>	17.2
Completeness [%]	99.9	99.8
Redundancy	4.83	4.83

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	18 *	Ferguson, A.D., (1998) Protein Sci., 7, 1636. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-20 (mg/ml)
2	1	reservoir	PEG6000	13-16 (%)
3	1	reservoir	sodium cacodylate	100 (mM)