2RC4

Crystal Structure of the HAT domain of the human MOZ protein

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-11
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9795, 1.2571, 1.2829, 1.2832
Spacegroup name	I 4 2 2
Unit cell lengths	109.200, 109.200, 144.779
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 3.000
R-factor	0.277
Rwork	0.276
R-free	0.28300
Structure solution method	MAD
RMSD bond length	0.009
RMSD bond angle	1.505
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE (2.03)
Refinement software	REFMAC (refmac_5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.770
High resolution limit [Å]	2.670	5.750	2.670
Rmerge	0.082	0.067	0.072
Number of reflections	12178
<I/σ(I)>	13.6
Completeness [%]	95.2	94.7	62.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	298	sodium cacodylate, PEG 3350, pH 6.5, VAPOR DIFFUSION, temperature 298K
1	VAPOR DIFFUSION	6.5	298	sodium cacodylate, PEG 3350, pH 6.5, VAPOR DIFFUSION, temperature 298K