3R38

2.23 Angstrom resolution crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (murA) from Listeria monocytogenes EGD-e

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	2011-02-17
Detector	MARMOSAIC 225 mm CCD
Spacegroup name	C 1 2 1
Unit cell lengths	144.579, 51.923, 78.178
Unit cell angles	90.00, 110.95, 90.00

Refinement procedure

Resolution	29.110 - 2.230
R-factor	0.19841
Rwork	0.196
R-free	0.23864
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2rl2
RMSD bond length	0.007
RMSD bond angle	1.328
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.290
High resolution limit [Å]	2.230	2.230
Rmerge	0.083	0.360
Number of reflections	26370
<I/σ(I)>	14.33	3.69
Completeness [%]	99.9	100
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	297	7.6 mg/mL protein in 10 mM Tris-HCl, 0.25 M sodium chloride, 5 mM BME. Crystallization condition: The Classics II Suite condition A5 (0.1 M HEPES, pH 7.5, 2 M ammonium sulfate). Cryo condition: 1:1 v/v 3.6 M ammonium sulfate : 50 % sucrose, VAPOR DIFFUSION, SITTING DROP, temperature 297K