1E6N

Chitinase B from Serratia marcescens inactive mutant E144Q in complex with N-acetylglucosamine-pentamer

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2000-03-27
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	55.732, 104.476, 186.676
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.580 - 2.250
R-factor	0.189
Rwork	0.189
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e15
RMSD bond length	0.010
RMSD bond angle	23.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.046	0.195
Total number of observations	123855 *
Number of reflections	47907	3349 *
<I/σ(I)>	22.6	4.7
Completeness [%]	89.8	63.1
Redundancy	2.6	2.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.6 *		Van Aalten, D.M.F., (2000) Proc. Natl. Acad. Sci. U.S.A., 97, 5842. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	citrate	50 (mM)
3	1	reservoir		0.5 (M)
4	1	reservoir	ammonium sulfate	0.25 (M)