1C7T

BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-11-12
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	109.174, 99.416, 86.556
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.900
R-factor	0.191 *
Rwork	0.191
R-free	0.24600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c7s
RMSD bond length	0.029 *
RMSD bond angle	0.032
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (/ ARP)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.000	1.970
High resolution limit [Å]	1.850 *	1.800 *
Rmerge	0.055	0.216 *
Total number of observations	1001880 *
Number of reflections	71983
<I/σ(I)>	10122.5
Completeness [%]	96.9	94
Redundancy		2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8		CO-CRYSTALS WERE GROWN BY THE HANGING-DROP VAPOR DIFFUSION METHOD. RESERVOIR BUFFER CONTAINED 2.3 MOLAR AMMONIUM SULFATE AND 100 MILLIMOLAR CACODYLATE BUFFER PH 4.8. PROTEIN SOLUTION 40 MILLIGRAM PER MILLILITER WAS MIXED WITH AN EQUAL VOLUME OF RESERVOIR CONTAINING 10 MILLIMOLAR DI-NAG. CRYSTALS ABOUT 0.5 X 0.2 X 0.2 MILLIMETER IN SIZE WERE FORMED WITHIN 2-3 DAYS., VAPOR DIFFUSION, HANGING DROP

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2.3 (M)
2	1	reservoir	cacodylate	100 (mM)
3	1	drop	protein	40 (mg/ml)
4	1	drop	diNAG	10 (mM)