1S5P

Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Wavelength(s)	0.9
Spacegroup name	P 41 21 2
Unit cell lengths	93.911, 93.911, 61.488
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 1.960
R-factor	0.234
Rwork	0.234
R-free	0.27000
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	1.260 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.030
High resolution limit [Å]	1.960	1.960
Rmerge	0.033	0.066 *
Number of reflections	20061
<I/σ(I)>	55.5	6.4
Completeness [%]	98.7	98 *
Redundancy	8.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5 *
1	Vapor diffusion, hanging drop *	6.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	cobB	10 (mg/ml)
2	1	drop	peptide	1.0 (mM)
3	1	reservoir	PEG3350	25 (%)
4	1	reservoir	Bis-Tris	100 (mM)	pH6.5