3N2L

2.1 Angstrom resolution crystal structure of an Orotate Phosphoribosyltransferase (pyrE) from Vibrio cholerae O1 biovar eltor str. N16961

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	2010-04-14
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 1 21 1
Unit cell lengths	96.587, 76.712, 133.944
Unit cell angles	90.00, 92.63, 90.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.22436
Rwork	0.222
R-free	0.26861
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lh0
RMSD bond length	0.015
RMSD bond angle	1.567
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.079	0.495
Number of reflections	114128
<I/σ(I)>	11.25	2.72
Completeness [%]	99.7	99.6
Redundancy	3.9	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	295	7.5 mg/mL protein in 10 mM Tris/HCl pH 8.3 0.5 M NaCl, 5 mM BME. The crystallization condition is The Classics II Suite (#8) Cryo 5M NaCl + 50% sucrose. Crystals grew from 1:1 v/v drop. , VAPOR DIFFUSION, SITTING DROP, temperature 295K