1J1I

Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU ULTRAX 18
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-12-14
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	I 4 2 2
Unit cell lengths	130.268, 130.268, 84.491
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.570 - 1.860
R-factor	0.215
Rwork	0.215
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iup
RMSD bond length	0.006
RMSD bond angle	22.800 *
Data reduction software	CrystalClear (1.3)
Data scaling software	CrystalClear (V. 1.3 (MSC/RIGAKU))
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.220	1.930
High resolution limit [Å]	1.860	1.860
Rmerge	0.073	0.286
Number of reflections	30496
<I/σ(I)>	6.8	2.4
Completeness [%]	99.2	98.6
Redundancy	4.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	20 *	PEG 6000, citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	5.2 (%)
2	1	reservoir	citric acid	26 (mM)	pH5.0
3	1	drop	protein	15-20 (mg/ml)