1O97

Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Collection date	2002-05-15
Spacegroup name	P 61
Unit cell lengths	118.248, 118.248, 85.216
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 1.600
R-factor	0.203
Rwork	0.201
R-free	0.22900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.020 *
RMSD bond angle	1.840 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.08)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.650
High resolution limit [Å]	1.600	1.600
Rmerge	0.069	0.285 *
Total number of observations	876371 *
Number of reflections	85935
<I/σ(I)>	16.1	2.7
Completeness [%]	96.3	95.5
Redundancy	5.2	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		2.5 M POTASSIUM PHOSPHATE PH 6.3

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG20000	30 (%(w/v))
2	1	reservoir	sodium acetate	0.2 (M)
3	1	reservoir	MES	0.1 (M)	pH6.5