1N31

Structure of A Catalytically Inactive Mutant (K223A) of C-DES with a Substrate (Cystine) Linked to the Co-Factor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Wavelength(s)	1.05
Spacegroup name	P 21 21 21
Unit cell lengths	62.681, 65.843, 172.563
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.920 - 2.200
R-factor	0.196
Rwork	0.196
R-free	0.25700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1elq
RMSD bond length	0.009 *
RMSD bond angle	1.380 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall
Low resolution limit [Å]	19.920
High resolution limit [Å]	2.200
Rmerge	0.062 *
Number of reflections	35389
Completeness [%]	95.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.6 *	20 *	citric acid, potassium phosphate, ammonium sulfate, peg8000, cystine(solid), pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10.3 (mg/ml)
2	1	drop	MOPS	10 (mM)	pH7.6
3	1	reservoir	potassium phosphate	100 (mM)
4	1	reservoir	citric acid	50 (mM)
5	1	reservoir	PEG8000	27 (%(w/v))
6	1	reservoir	ammonium sulfate	100 (mM)	pH6.5