4V2I

Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium Thalassospira sp

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	CCD
Collection date	2013-02-08
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	73.326, 85.429, 91.747
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.866 - 1.686
R-factor	0.1451
Rwork	0.143
R-free	0.18210
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qz3
RMSD bond length	0.008
RMSD bond angle	1.177
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.790
High resolution limit [Å]	1.690	1.690
Rmerge	0.100	0.620
Number of reflections	61330
<I/σ(I)>	13.6	2.4
Completeness [%]	93.4	63.3
Redundancy	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		8		THE PROTEIN WAS AT 10 MG/ML IN 50 MM TRIS-HCL PH 8.0, 500 MM NACL AND 10% GLYCEROL. RESERVOIR: 25% PEG 3350, 0.2 M MGCL2