1CY5

CRYSTAL STRUCTURE OF THE APAF-1 CARD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X26C
Synchrotron site	NSLS
Beamline	X26C
Temperature [K]	100
Detector technology	CCD
Collection date	1999-02-01
Detector	ADSC
Spacegroup name	P 21 21 21
Unit cell lengths	36.350, 46.910, 54.350
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 1.300
R-factor	0.169
R-free	0.19900
Structure solution method	MAD PROGRAM PACKAGE USED (IF ANY) : SHARP STARTING MODEL FOR MOLECULAR REPLACEMENT: NONE
RMSD bond length	0.005
RMSD bond angle	0.019
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.350
High resolution limit [Å]	1.300	1.300
Rmerge	0.026 *	0.230
Total number of observations	145226 *
Number of reflections	24113
<I/σ(I)>	35	2.3
Completeness [%]	98.0	96
Redundancy	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8	290	HANGING DROP VAPOR DIFFUSION WITH EQUAL VOLUMES OF PROTEIN AND RESERVOIR SOLUTIONS. PROTEIN SOLUTION: 5-20 MG/ML PROTEIN IN 0.02 MOLAR TRIS (PH 8.0-8.5) , 0.1-0.2 MOLAR SODIUM CHLORIDE. 0.005 MOLAR 2-MERCAPTOETHANOL RESERVOIR SOLUTION: 8-20% (W/V) PEG 8000, 0.2 MOLAR TRIS (PH 7.5-8.0), 0.05-0.2 MOLAR ZINC ACETATE., VAPOR DIFFUSION, HANGING DROP, temperature 17K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	zinc