1BO4

CRYSTAL STRUCTURE OF A GCN5-RELATED N-ACETYLTRANSFERASE: SERRATIA MARESCENS AMINOGLYCOSIDE 3-N-ACETYLTRANSFERASE

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F2
Synchrotron site	CHESS
Beamline	F2
Temperature [K]	100
Detector technology	CCD
Collection date	1998-05-15
Wavelength(s)	0.9793, 0.9703, 0.9668
Spacegroup name	C 1 2 1
Unit cell lengths	78.540, 102.260, 50.140
Unit cell angles	90.00, 93.73, 90.00

Refinement procedure

Resolution	15.000 - 2.300
R-factor	0.201
Rwork	0.201
R-free	0.25000
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	24.000 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS (0.3C)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.052 *	0.093 *
Total number of observations	118408 *
Number of reflections	16291
<I/σ(I)>	7.6	6.4
Completeness [%]	92.9	92.9
Redundancy	7.3	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8	4 *	SITTING DROP, 4 DEGREES C, 3.5MG/ML PROTEIN + 5MM COA, 100MM TRIS-HCL PH7.8, 0.8% PEG4K, 18% T-BUTANOL, 20MM SRCL2, 7% DIOXANE, 5% 2,4-METHYLPENTANEDIOL, 40MM HEXANEDIOL, 10MM DITHIOTHREITOL, 2MM TRIS(2-CARBOXY- ETHYL)PHOSPHINE-HCL, 10MM SPERMIDINE, 2.5% GLYCEROL, vapor diffusion - sitting drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.5 (mg/ml)
10	1	reservoir	dithiothreitol	10 (mM)
11	1	reservoir	tri(2-carboxyethyl)phosphine-HCl	2 (mM)
12	1	reservoir	spermidine	10 (mM)
13	1	reservoir	glycerol	2.5 (%)
2	1	drop	CoA	5 (mM)
3	1	reservoir	Tris-HCl	100 (mM)
4	1	reservoir	PEG4000	0.8 (%)
5	1	reservoir	t-butanol	18 (%)
6	1	reservoir		20 (mM)
7	1	reservoir	dioxane	7 (%)
8	1	reservoir	MPD	50 (%)
9	1	reservoir	hexanediol	40 (mM)