4H19

Crystal structure of an enolase (mandelate racemase subgroup, target EFI-502087) from agrobacterium tumefaciens, with bound Mg and d-ribonohydroxamate, ordered loop

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	2011-07-11
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	C 2 2 21
Unit cell lengths	178.363, 395.688, 177.802
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	197.840 - 1.800
R-factor	0.139
Rwork	0.137
R-free	0.17550
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tj4
RMSD bond length	0.020
RMSD bond angle	1.851
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.16)
Phasing software	PHENIX
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	197.844	197.844	1.900
High resolution limit [Å]	1.800	5.690	1.800
Rmerge		0.066	0.649
Total number of observations		135941	483636
Number of reflections	573535
<I/σ(I)>	10	6.2	1.2
Completeness [%]	100.0	99.5	99.9
Redundancy	6.7	7.2	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffuction	4	298	Protein (10 mM Tris, pH 8.0, 200 mM NaCl, 5 mM Mg, 10 mM D-ribonohydroxamate; Reservoir (20% (w/v) PEG-8000, 100 mM Tris pH 8.5, 200 mM MgCl2); Cryoprotection (Reservoir, + 20% glycerol, 50 mM MgCl, 10 mM D-ribonohydroxamate), sitting drop vapor diffuction, temperature 298K