4N1L

Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Collection date	2012-10-08
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.87260
Spacegroup name	P 21 21 2
Unit cell lengths	51.350, 62.550, 29.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.689 - 1.986
R-factor	0.1841
Rwork	0.182
R-free	0.22170
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NLRP14 PYD Ser6-Pro67
RMSD bond length	0.007
RMSD bond angle	1.029
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	PHENIX ((phenix.refine: 1.8.3_1479))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.720	2.090
High resolution limit [Å]	1.986	1.986
Number of reflections	6916
Completeness [%]	100.0	100
Redundancy	6.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	293	0.2 M Ammonium acetate and 2.2 M Ammonium sulfate , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K