1K3B

Crystal Structure of Human Dipeptidyl Peptidase I (Cathepsin C): Exclusion Domain Added to an Endopeptidase Framework Creates the Machine for Activation of Granular Serine Proteases

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1998-06-30
Detector	MARRESEARCH
Wavelength(s)	1.0
Spacegroup name	I 2 2 2
Unit cell lengths	87.154, 88.031, 114.609
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.150
R-factor	0.186
Rwork	0.190
R-free	0.23100
Structure solution method	MAD, MIR, MOL. REPL together
RMSD bond length	0.009
RMSD bond angle	1.540
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	MAIN

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.180
High resolution limit [Å]	2.150	2.150
Rmerge	0.070	0.249 *
Total number of observations	96833 *
Number of reflections	23553
Completeness [%]	97.6	99 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	293	ammonium sulphate, sodium citrate, potassium/sodium tartrate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium sulfate	2.0 (M)
3	1	reservoir	sodium citrate	0.1 (M)
4	1	reservoir	potassium/sodium tartrate	0.2 (M)	pH5.6