5IDI

Structure of beta glucosidase 1A from Thermotoga neapolitana, mutant E349A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2011-04-12
Detector	MARRESEARCH
Wavelength(s)	1.0402
Spacegroup name	P 21 21 21
Unit cell lengths	67.277, 98.726, 154.756
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.900
R-factor	0.17082
Rwork	0.169
R-free	0.21470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cbv
RMSD bond length	0.027
RMSD bond angle	2.240
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.100	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.084	1.172
Number of reflections	81717
<I/σ(I)>	12.6	1.9
Completeness [%]	99.1	85.4
Redundancy	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	5	288	Protein at 12 mg/ml in 20 mM citrate phosphate buffer, pH 5.6. Hanging drops consisting of 1 microlitre of protein solution and 2 microlitres of reservoir solution (18-23% w/v PEG 6000, 0.2 M sodium chloride, 0.1 M sodium acetate, pH 5.0) equilibrated against 1 ml of reservoir solution. Rod-shaped crystals of approximate dimensions 0.3 x 0.2 x 0.3 mm grew after 8-10 days.