1SC4

Crystal structure of the human caspase-1 C285A mutant after removal of malonate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	180
Detector technology	IMAGE PLATE
Collection date	2003-07-10
Detector	RIGAKU RAXIS IV
Spacegroup name	P 43 21 2
Unit cell lengths	62.982, 62.982, 143.158
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.22295
Rwork	0.221
R-free	0.25840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rwn
RMSD bond length	0.006
RMSD bond angle	0.911
Data reduction software	CrystalClear ((MSC/RIGAKU))
Data scaling software	d*TREK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.110	0.297
Number of reflections	17527
Completeness [%]	95.3	78.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	274	2 M sodium malonate, VAPOR DIFFUSION, HANGING DROP, temperature 274K. Malonate-bound enzyme crystals were transferred into mother liquor composed of 0.1 M PIPES pH 6, 88 mM (NH4)2SO4, 25% PEG 2000 MME, 10 mM DTT, 3 mM NaN3 and 2 mM MgCl2, and soaked for 2 days to remove malonate.