3Q66

Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2009-02-10
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97934
Spacegroup name	P 61 2 2
Unit cell lengths	99.385, 99.385, 479.605
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.505 - 2.705
R-factor	0.2066
Rwork	0.206
R-free	0.24750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB entries 3CZ7 2ZD7
RMSD bond length	0.011
RMSD bond angle	1.196
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.6.1_357))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.750
High resolution limit [Å]	2.700	2.700
Rmerge	0.094	0.906
Number of reflections	37636
<I/σ(I)>	34.1	5.3
Completeness [%]	99.4	99.9
Redundancy	16.8	17.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	277	0.1 M sodium citrate tribasic dihydrate, 2 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K