5UTP

Crystal structure of Burkholderia cenocepacia family 3 glycoside hydrolase (NagZ) bound to N-ethylbutyryl-PUGNAc

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2013-09-25
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	51.210, 85.890, 65.610
Unit cell angles	90.00, 102.79, 90.00

Refinement procedure

Resolution	25.230 - 2.200
Rwork	0.175
R-free	0.22580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4g6c
RMSD bond length	0.002
RMSD bond angle	0.623
Data reduction software	iMOSFLM
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((dev_2236))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.940	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.137	0.249
Number of reflections	27671	2380
<I/σ(I)>	5.1	3.1
Completeness [%]	98.2	98
Redundancy	2.9	2.8
CC(1/2)	0.950	0.908

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	30-32% PEG8000, 0.1 M MES, pH 6.2-6.8