3RM3

Crystal structure of monoacylglycerol lipase from Bacillus sp. H257

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	CCD
Collection date	2010-07-03
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	38.150, 71.210, 43.660
Unit cell angles	90.00, 111.70, 90.00

Refinement procedure

Resolution	17.723 - 1.200
R-factor	0.1358
Rwork	0.135
R-free	0.15790
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1r1d
RMSD bond length	0.007
RMSD bond angle	1.191
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.9)
Phasing software	BALBES
Refinement software	PHENIX (1.7_650)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.566	17.723	1.260
High resolution limit [Å]	1.200	3.790	1.200
Rmerge		0.048	0.346
Number of reflections	67545
<I/σ(I)>	10.7	11.4	2.2
Completeness [%]	99.8	96.6	99.8
Redundancy	3.7	3.6	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	0.1 M MES/imidazole pH 6.5, 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD, and 0.02 M of monosaccharides (D-glucose, D-mannose, D-galactose, L-fuctose, D-xylose, and N-acetyl-D-glucosamine), VAPOR DIFFUSION, SITTING DROP, temperature 293K