3RIT

Crystal structure of Dipeptide Epimerase from Methylococcus capsulatus complexed with Mg and dipeptide L-Arg-D-Lys

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2010-03-18
Detector	RAYONIX MX-300
Wavelength(s)	0.9786
Spacegroup name	I 21 3
Unit cell lengths	275.320, 275.320, 275.320
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.870 - 2.701
R-factor	0.1775
Rwork	0.175
R-free	0.22150
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.339
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: dev_721))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.870	19.870	2.800
High resolution limit [Å]	2.700	5.770	2.700
Rmerge	0.154	0.031	0.775
Number of reflections	94319
<I/σ(I)>	12.84	31.57	2.03
Completeness [%]	99.7	97.3	100
Redundancy	21.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	277	Precipitant contained 25% PEG 3350, 0.1M Tris-HCl, and 0.2M Li2SO4. Protein solution contained 0.1M KCl, 0.05M HEPES (pH 8.0), 0.02M L-Arg-L-Lys, and 0.01M MgCl2. Protein concentration was 12 mg/mL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K