2Y2W

Elucidation of the substrate specificity and protein structure of AbfB, a family 51 alpha-L-arabinofuranosidase from Bifidobacterium longum.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2009-04-25
Detector	ADSC QUANTUM 315r
Spacegroup name	P 21 21 21
Unit cell lengths	108.469, 165.811, 184.297
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.500
R-factor	0.22263
Rwork	0.220
R-free	0.26986
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pz3
RMSD bond length	0.006
RMSD bond angle	0.920
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.640
High resolution limit [Å]	2.500	2.500
Rmerge	0.120	0.560
Number of reflections	109183
<I/σ(I)>	8.9	2.4
Completeness [%]	99.8	100
Redundancy	4.1	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION			ABFB CRYSTALS WERE OBTAINED BY MIXING 1 MICROLITER CONCENTRATED PROTEIN SOLUTION WITH 3 MICROLITER CRYSTALLIZATION SOLUTION CONTAINING 0.2 M SODIUM PHOSPHATE MONOBASIC MONOHYDRATE, 20% W/V POLYETHYLENE GLYCOL 3350, USING THE VAPOR-DIFFUSION METHOD WITH HANGING OR SITTING DROPS AT 20-24 C.