4GNV

Crystal structure of beta-hexosaminidase 1 from Burkholderia cenocepacia J2315 with bound N-Acetyl-D-Glucosamine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-29
Detector	ADSC QUANTUM 315
Wavelength(s)	0.976484
Spacegroup name	P 1 21 1
Unit cell lengths	48.970, 89.310, 67.150
Unit cell angles	90.00, 91.73, 90.00

Refinement procedure

Resolution	67.120 - 1.500
R-factor	0.1493
Rwork	0.148
R-free	0.17550
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.456
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	67.120	1.539
High resolution limit [Å]	1.500	1.500
Rmerge	0.041	0.229
Number of reflections	85727
<I/σ(I)>	28.22	4.57
Completeness [%]	97.8	84.57
Redundancy	6.11

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	289	EBS Internal tracking number 234629b12: BuceA.18451.a.B1.PW36254 at 20 mg/mL in 25 mM HEPES (pH 7.0), 500 mM NaCl, 2 mM DTT, 0.025% Sodium Azide, 5% glycerol. 0.4 uL x 0.4 uL drop with Morpheus Screen B12: 90 mM Halogens (NaF, NaBr, NaI), 0.1 M Tris/Bicine pH 8.5, 37.5% MPD-PEG1000-PEG3500, SOAK 1 week with 10 mM N-acetyl-D-glucosamine, VAPOR DIFFUSION, SITTING DROP, temperature 289K