1PU9

Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Detector technology	CCD
Collection date	2000-06-08
Detector	ADSC QUANTUM 210
Spacegroup name	P 32 2 1
Unit cell lengths	64.730, 64.730, 96.416
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 2.300
R-factor	0.236
Rwork	0.236
R-free	0.27700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qsn
RMSD bond length	0.021 *
RMSD bond angle	2.640 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	2.390
High resolution limit [Å]	2.210 *	2.210 *
Rmerge	0.092 *	0.180 *
Total number of observations	67990 *
Number of reflections	22051 *
Completeness [%]	99.5 *	99.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	20 *	Ammonium sulfate, MnCl2, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	tGCN5	0.4 (mM)
2	1	drop	CoA	1.0 (mM)
3	1	drop	H3-derived peptide	1.5 (mM)
4	1	reservoir	ammonium sulfate	1.6 (M)
5	1	reservoir		10-50 (mM)
6	1	reservoir	Tris	50 (mM)	pH7.5