4AFM

Structural and biochemical characterization of a novel Carbohydrate Binding Module of endoglucanase Cel5A from Eubacterium cellulosolvens.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 1
Synchrotron site	SOLEIL
Beamline	PROXIMA 1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-04-04
Detector	ADSC QUANTUM 315r
Spacegroup name	P 61 2 2
Unit cell lengths	48.740, 48.740, 193.720
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.700 - 1.250
R-factor	0.15874
Rwork	0.158
R-free	0.17306
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4aek
RMSD bond length	0.031
RMSD bond angle	2.873
Data reduction software	iMOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.740	1.320
High resolution limit [Å]	1.250	1.250
Rmerge	0.070	0.400
Number of reflections	35557
<I/σ(I)>	28.2	4
Completeness [%]	91.2	62.4
Redundancy	21.6	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		4.6	292	80 MG/ML OF PROTEIN AT 292 K WERE GROWN IN 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.6, 26% W/V PEG 2K MME. CRYSTALS WERE SOAKED WITH 10 MM CELLOHEXAOSE FOR A FEW HOURS. 30% GLYCEROL WAS USED AS A CRYOPROTECTANT.