3UGV

Crystal structure of an enolase from alpha pretobacterium bal199 (EFI TARGET EFI-501650) with bound MG

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2011-07-27
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	152.711, 152.984, 173.535
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	114.642 - 2.300
R-factor	0.1628
Rwork	0.161
R-free	0.20770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mdr
RMSD bond length	0.012
RMSD bond angle	1.054
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.16)
Phasing software	PHENIX
Refinement software	PHENIX (1.7_650)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	173.535	152.984	2.420
High resolution limit [Å]	2.300	7.270	2.300
Rmerge	0.077	0.024	0.481
Total number of observations		24837	92528
Number of reflections	175465
<I/σ(I)>	11.9	25.3	1.6
Completeness [%]	97.7	97.5	96.6
Redundancy	4.3	4.2	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	298	Protein (10 mM Hepes, pH 7.8, 150 mM NaCl, 10% glycerol, 5 mM DTT, 5 mM MgCl2); Reservoir (200 mM MgAcetate, 100 mM NaCac pH 6.5, 30% MPD); Cryoprotection (Reservoir), VAPOR DIFFUSION, SITTING DROP, temperature 298K