3T52

L29I Mutation in an Aryl Esterase from Pseudomonas fluorescens Leads to Unique Peptide Flip and Increased Activity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-05-10
Detector	NOIR-1
Wavelength(s)	0.98
Spacegroup name	P 32
Unit cell lengths	146.020, 146.020, 128.950
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.800 - 2.000
R-factor	0.185
Rwork	0.184
R-free	0.21080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	IVA4
RMSD bond length	0.015
RMSD bond angle	1.368
Data reduction software	d*TREK (9.9.3L)
Data scaling software	d*TREK (9.9.3L)
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.330	48.330	2.070
High resolution limit [Å]	2.000	4.310	2.000
Rmerge	0.111	0.069	0.427
Total number of observations		117313	111064
Number of reflections	207756
<I/σ(I)>	6.6	13.7	2.9
Completeness [%]	100.0	99.9	100
Redundancy	5.46	5.6	5.26

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	1% PEG 400, 1.65M (NH4)2SO4, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K