3Q33

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2008-12-14
Detector	MARMOSAIC 300 mm CCD
Spacegroup name	P 21 21 2
Unit cell lengths	97.543, 119.570, 80.566
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.160 - 2.800
R-factor	0.195
Rwork	0.195
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENTRIES 3D35 3DM7
RMSD bond length	0.009
RMSD bond angle	1.154
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	PHENIX (phenix.refine: 1.6.4_486)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.850
High resolution limit [Å]	2.750	2.750
Number of reflections	23924
<I/σ(I)>	26.1	2.4
Completeness [%]	94.9	78.1
Redundancy	4.8	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5	298	10.0% (v/v) PEG 8000 8% (v/v) ethylene glycol 100 mM Hepes, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.5