4Q3L

Crystal structure of MGS-M2, an alpha/beta hydrolase enzyme from a Medee basin deep-sea metagenome library

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2014-03-28
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	105.568, 139.134, 111.109
Unit cell angles	90.00, 89.94, 90.00

Refinement procedure

Resolution	31.669 - 3.010
R-factor	0.2029
Rwork	0.201
R-free	0.25540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cr6
RMSD bond length	0.004
RMSD bond angle	0.711
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	PHENIX ((phenix.refine: dev_1631))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.000	3.050
High resolution limit [Å]	3.000	3.000
Rmerge	0.093	0.536
Number of reflections	63183
<I/σ(I)>	17.08	3.66
Completeness [%]	99.9	100
Redundancy	4.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	protein treated with thermolysin in 1/10 molar ratio crystallization in: 0.1 M sodium Hepes, 1.4 M sodium citrate, cryoprotectant: 15% ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K