5KTT

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound L-malate and Fe4S4 cluster

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2013-04-05
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97925
Spacegroup name	P 1 21 1
Unit cell lengths	47.333, 54.639, 55.613
Unit cell angles	90.00, 90.79, 90.00

Refinement procedure

Resolution	29.943 - 1.500
R-factor	0.1485
Rwork	0.146
R-free	0.19260
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5ktn
RMSD bond length	0.011
RMSD bond angle	1.846
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX ((1.10_2155: 000))
Refinement software	PHENIX ((1.10_2155: 000))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.046	0.484
Number of reflections	44361
<I/σ(I)>	15.9	2.7
Completeness [%]	97.3	99.9
Redundancy	2.9	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		296	210 mM ammonium chloride, 8 - 15% polyethylene glycol 4000, and 40 mM HEPES, pH 5.5 - 7.5. L-malic acid, pH 5.6, was added to the protein solution to a final concentration of 10 mM