5CML

Crystal structure of the Esterase domain from Rhodothermus marinus Rmar_1206 protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I02
Synchrotron site	Diamond
Beamline	I02
Temperature [K]	100
Detector technology	PIXEL
Collection date	2013-07-25
Detector	DECTRIS PILATUS 2M
Wavelength(s)	0.9795
Spacegroup name	P 1 21 1
Unit cell lengths	60.325, 74.069, 60.953
Unit cell angles	90.00, 113.47, 90.00

Refinement procedure

Resolution	44.620 - 1.560
R-factor	0.1458
Rwork	0.144
R-free	0.17620
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2fuk 3trd 3pf9
RMSD bond length	0.010
RMSD bond angle	1.179
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.620	1.612
High resolution limit [Å]	1.560	1.560
Rmerge	0.044	0.725
Number of reflections	69888
<I/σ(I)>	13.91	1.88
Completeness [%]	99.1	98.48
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	298	Protein at 15 mg/ml was crystallized by sitting drop vapour diffusion with 100 nl drops of protein supplemented with 100 nl of mother liquor comprising 0.2 M ammonium citrate dibasic, pH 5.0, 20 % w/v PEG 3350 (Hampton PEG/Ion HT96 screen D12), drops were equilibrated against 70 ul of mother liquor for one month before crystals appeared.