1G96

HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-09-30
Detector	MARRESEARCH
Wavelength(s)	0.8423
Spacegroup name	I 4 3 2
Unit cell lengths	140.530, 140.530, 140.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.500
R-factor	0.216
Rwork	0.220
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	N-terminally truncated chicken cystatin (1cew.pdb) converted to a polyalanine chain and limited to those fragments that had been modeled in electron density (residues 86-90 not included)
RMSD bond length	0.015
RMSD bond angle	25.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.070	0.413
Total number of observations	167936 *
Number of reflections	8429
<I/σ(I)>	27.8	2.5
Completeness [%]	99.2	93.5
Redundancy	19.9	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8	277	Lyophilized protein was dissolved in 100 mM sodium acetate buffer pH 4.8 containing 20 mM CaCl2. Droplets were equilibrated against 1 ml of reservoir with analogous buffer/CaCl2 solution. After 2 and 4 days, the reservoir solution was supplemented with 100 microliters of MPD, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium acetate	100 (mM)
3	1	drop		20 (mM)
4	1	reservoir	MPD