1PZW

Crystal structure of the zinc finger associated domain of the Drosophila transcription factor Grauzone

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-10
Detector	MARRESEARCH
Wavelength(s)	1.0500, 1.2828
Spacegroup name	P 41 21 2
Unit cell lengths	48.660, 48.660, 82.123
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.000
R-factor	0.24204
Rwork	0.241
R-free	0.26700 *
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	1.200 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	REFMAC (5.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.000
High resolution limit [Å]	1.950	1.950
Number of reflections	6907
<I/σ(I)>	36.7	6.3
Completeness [%]	97.0	99.7
Redundancy	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	22 *	PEG 4000, ammonium acetate, sodium citrate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	reservoir	ammonium acetate	0.2 (M)
3	1	reservoir	sodium citrate	0.1 (M)	pH5.6
4	1	reservoir	PEG4000	30 (%)