3PAJ

2.00 Angstrom resolution crystal structure of a quinolinate phosphoribosyltransferase 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	2010-10-14
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	59.195, 79.551, 117.908
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.600 - 2.000
R-factor	0.17557
Rwork	0.173
R-free	0.22175
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qap
RMSD bond length	0.013
RMSD bond angle	1.609
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	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.081	0.279
Number of reflections	38142
<I/σ(I)>	22.98	9.76
Completeness [%]	99.8	100
Redundancy	7.1	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	287	Protein: 7 mg/mL in 10 mM Tris/HCl pH 8.3, 0.5 M NaCl, 5 mM BME. Crystallization condition: 0.2 M MgCl2, 0.1 M Bis-Tris, 25 % (w/v) PEG3350. Mixed 1:1 v/v., VAPOR DIFFUSION, SITTING DROP, temperature 287K