1EHN

CRYSTAL STRUCTURE OF CHITINASE A MUTANT E315Q COMPLEXED WITH OCTA-N-ACETYLCHITOOCTAOSE (NAG)8.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-04-04
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	200.440, 131.617, 59.344
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.900
R-factor	0.173 *
Rwork	0.173
R-free	0.21700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1edq
RMSD bond length	0.012
RMSD bond angle	0.028
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.050	0.242 *
Number of reflections	61168
<I/σ(I)>	16.5	5.9
Completeness [%]	99.0	100
Redundancy	4.1	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	18 *	0.75 M CITRATE-NA PH 7.2 AND 20% (V/V) METHANOL, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	sodium citrate	0.75 (M)
3	1	reservoir	methanol	20 (%(v/v))