4EMB

Crystal structure of a phosphoglycerate mutase gpmA from Borrelia burgdorferi B31

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-21
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	77.320, 116.750, 84.410
Unit cell angles	90.00, 107.67, 90.00

Refinement procedure

Resolution	50.000 - 2.300
R-factor	0.1775
Rwork	0.176
R-free	0.20130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3lnt
RMSD bond length	0.013
RMSD bond angle	1.442
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.360
High resolution limit [Å]	2.300	10.290	2.300
Rmerge	0.078	0.044	0.473
Number of reflections	63406	730	4697
<I/σ(I)>	18.97	40.64	4.78
Completeness [%]	99.9	97.9	99.9
Redundancy	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	BobuA.01013.a.A1 selenomethionine-labeled PW26571 at 27.7 mg/mL against CSHT B6: 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, 20% PEG8000, cryoprotectant: 20% ethylene glycol, crystal tracking ID 232024b6, VAPOR DIFFUSION, SITTING DROP, temperature 289K