5U9T

The Tris-thiolate Zn(II)S3Cl Binding Site Engineered by D-Cysteine Ligands in de Novo Three-stranded Coiled Coil Environment

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-11
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	76.119, 28.977, 43.917
Unit cell angles	90.00, 119.83, 90.00

Refinement procedure

Resolution	26.530 - 1.920
R-factor	0.198
Rwork	0.197
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3h5f
RMSD bond length	0.010
RMSD bond angle	1.090
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	26.530	50.000	1.990
High resolution limit [Å]	1.920	4.140	1.920
Rmerge	0.060	0.045	0.207
Total number of observations	21879
Number of reflections	6290
<I/σ(I)>	15.2
Completeness [%]	96.7	95.4	84.9
Redundancy	3.5	3.2	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	Peptide sample: 13.2 mg/mL peptide, 15 mM Zn(OAc)2, 5mM TRIS buffer pH 8.5 Crystallization well condition: 40% PEG 400, 0.1M Acetate buffer pH 4.6 (final pH 5.4)