4CIB

crystal structure of cathepsin a, complexed with compound 2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-08-29
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	89.649, 102.527, 49.395
Unit cell angles	90.00, 100.94, 90.00

Refinement procedure

Resolution	44.020 - 1.890
R-factor	0.14484
Rwork	0.141
R-free	0.21073
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4az0
RMSD bond length	0.013
RMSD bond angle	1.409
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.740	1.940
High resolution limit [Å]	1.890	1.890
Rmerge	0.080	0.350
Number of reflections	35026
<I/σ(I)>	14.12	3.76
Completeness [%]	99.9	100
Redundancy	3.8	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	277	CATHEPSIN A WAS CRYSTALLIZED USING THE HANGING DROP METHOD: 1 UL OF PROTEIN SOLUTION, CONTAINING 6.5 MG/ML CATHEPSIN A, 25 MM TRIS-HCL (PH 8.0) AND 300 MM NACL, WAS MIXED WITH 1 UL RESERVOIR SOLUTION, CONTAINING 100 MM NAACETATE (PH 4.5), 18-20% PEG400 AND 100 MM CDCL2, AND SET TO EQUILIBRATE AT 4DEG.C. ROD-SHAPED CRYSTALS APPEARED IN ABOUT ONE WEEK.