1QTN

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	105
Detector technology	CCD
Collection date	1998-09-09
Detector	BRUKER
Spacegroup name	P 31 2 1
Unit cell lengths	62.400, 62.400, 129.250
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 1.200
R-factor	0.143 *
Rwork	0.143
R-free	0.18800
Structure solution method	MR
Starting model (for MR)	1cp3
RMSD bond length	0.020
RMSD bond angle	0.200
Data reduction software	SMART
Data scaling software	SAINT
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.240
High resolution limit [Å]	1.200	1.200
Rmerge	0.068	0.260
Total number of observations	298890 *
Number of reflections	79890
<I/σ(I)>		2.35
Completeness [%]	87.0	82
Redundancy	3.73

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	4 *	3 MICROLITERS PROTEIN (8.4 MG/ ML IN 20 MM TRISHCL, 100MM DTT AT PH 8.0) MIXED WITH 3 MICROLITERS WELL BUFFER (1.4 SODIUM CITRATE, 0.1M HEPES, AT PH 8.0) AT 4 DEG. C, VAPOR DIFFUSION, SITTING DROP, temperature 282K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.4 (mg/ml)
2	1	drop	Tris	20 (mM)
3	1	drop	dithiothreitol	100 (mM)
4	1	reservoir	sodium citrate	1.4 (M)
5	1	reservoir	HEPES	0.1 (M)