4YXC

Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2014-09-23
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.075
Spacegroup name	P 21 21 21
Unit cell lengths	43.210, 76.370, 119.350
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.022 - 2.300
R-factor	0.2031
Rwork	0.197
R-free	0.26200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4YXB and 2LZM
RMSD bond length	0.009
RMSD bond angle	1.150
Data scaling software	Aimless (0.2.7)
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	64.330	64.330	2.380
High resolution limit [Å]	2.300	8.910	2.300
Rmerge	0.070	0.031	0.923
Rpim	0.020	0.010	0.260
Total number of observations	234350	4081	22662
Number of reflections	18223
<I/σ(I)>	20.2	57.2	2.6
Completeness [%]	99.8	96.7	99.8
Redundancy	12.9	11.2	12.9
CC(1/2)	0.999	0.999	0.811

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	FliM(245-334)::FliN(5-137) + FliH(1-18)::T4 lysozyme was concentrated to 17mg/mL and crystallized with 11% PEG400, 100mM sodium potassium phosphate pH=6.5. Crystals were cryoprotected with 40% PEG400, 200mM sodium potassium phosphate pH=6.5.