1GO4

Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF
Synchrotron site	ESRF
Temperature [K]	287
Detector technology	CCD
Collection date	2001-05-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	111.037, 63.023, 139.511
Unit cell angles	90.00, 111.65, 90.00

Refinement procedure

Resolution	24.500 - 2.050
R-factor	0.24
Rwork	0.240
R-free	0.26800
Structure solution method	SIRAS
Starting model (for MR)	1duj
RMSD bond length	0.015 *
RMSD bond angle	1.880 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SnB
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.180
High resolution limit [Å]	2.050	2.050
Rmerge	0.038	0.341 *
Total number of observations	368557 *
Number of reflections	113010
<I/σ(I)>	18.2	2.96
Completeness [%]	99.2	90
Redundancy	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.2	20 *	PROTEIN CONCENTRATION 7.5 MG/ML HANGING DROP METHOD, WELL=100 MM AMMONIUM SULPHATE, 100 MM AMMONIUM CITRATE PH 5.2, 10 MM DTT

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	reservoir	ammonium sulfate	100 (mM)
3	1	reservoir	sodium citrate	100 (mM)	pH5.2
4	1	reservoir	dithiothreitol	10 (mM)