2I3I

Structure of an ML-IAP/XIAP chimera bound to a peptidomimetic

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2005-02-21
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.54
Spacegroup name	P 41 21 2
Unit cell lengths	87.356, 87.356, 73.196
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.340 - 2.300
R-factor	0.18954
Rwork	0.188
R-free	0.22385
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1.3 A structure of the ML-IAP/XIAP protein bound to a different peptidomimetic with the ligand and surrounding waters removed
RMSD bond length	0.013
RMSD bond angle	1.363
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.169	0.597
Number of reflections	13095
<I/σ(I)>	11	3.4
Completeness [%]	99.8	100
Redundancy	6.1	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	Lithium sulfate, PEG 3350, Bis-tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K