1K4J

Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	113
Detector technology	CCD
Collection date	1999-11-13
Detector	BRANDEIS - B4
Wavelength(s)	1.14, 1.1724, 1.1719, 1.19
Spacegroup name	P 43
Unit cell lengths	66.390, 66.390, 47.325
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.500
R-factor	0.216 *
Rwork	0.216
R-free	0.27500
Structure solution method	MAD
Starting model (for MR)	none
RMSD bond length	0.008
RMSD bond angle	23.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.042 *	0.175 *
Total number of observations	32922 *
Number of reflections	7283 *
<I/σ(I)>	20.9	3.2
Completeness [%]	97.0	98.1
Redundancy	4.5	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.1	291	PEG 4000, 2-propanol, MES, EDTA, beta-mercaptoethanol, NaN3, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	reservoir	MES	0.1 (M)	pH6.1
3	1	reservoir	PEG4000	14 (%)
4	1	reservoir	isopropanol	6 (%)
5	1	reservoir	beta-mercaptoethanol	0.03 (%)
6	1	reservoir	EDTA	10 (mM)
7	1	reservoir		0.5 (%)