1C7S

BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-04-04
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	108.794, 99.960, 86.308
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.800
R-factor	0.183
Rwork	0.171
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qbb
RMSD bond length	0.022 *
RMSD bond angle	0.024
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (/ ARP)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.024	0.095
Total number of observations	937195 *
Number of reflections	76047
<I/σ(I)>	32832	4738
Completeness [%]	86.9 *	90.8

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)