3Q68

Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121)

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	2009-11-29
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97901
Spacegroup name	P 21 21 21
Unit cell lengths	90.988, 98.056, 171.366
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.137 - 2.705
R-factor	0.202
Rwork	0.202
R-free	0.22580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB entries 3CZ7 2ZD7
RMSD bond length	0.022
RMSD bond angle	1.545
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	0.072	0.904
Number of reflections	40782
<I/σ(I)>	28.4	2.5
Completeness [%]	99.6	100
Redundancy	8.1	8.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	277	1.8 M sodium citrate, 30% (w/v) 1,6-hexanediol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K