1NB3

Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	90
Detector technology	IMAGE PLATE
Collection date	2001-01-08
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	48.584, 91.630, 161.235
Unit cell angles	90.00, 93.69, 90.00

Refinement procedure

Resolution	10.000 - 2.800
Rwork	0.227
R-free	0.24600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1stf 8pch
RMSD bond length	0.012
RMSD bond angle	1.740
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	MAIN

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.161 *	0.583 *
Total number of observations	313477 *
Number of reflections	35154 *
<I/σ(I)>		4.7
Completeness [%]	97.4 *	97.1 *
Redundancy	8.9	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	4.2 *	22 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	18 (%(w/v))
2	1	reservoir	ammonium sulfate	0.18 (M)
3	1	reservoir	sodium acetate	0.1 (M)	pH4.2
4	1	drop	protein	7 (mg/ml)
5	1	drop		40 (mM)