4Q15

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Halofuginone and AMPPNP in space group P212121 at 2.35 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2014-03-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 21 21 21
Unit cell lengths	76.580, 78.090, 167.820
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	37.331 - 2.350
R-factor	0.1962
Rwork	0.195
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4olf
RMSD bond length	0.003
RMSD bond angle	0.757
Data scaling software	XSCALE
Phasing software	PHASER (2.5.6)
Refinement software	PHENIX (dev_1659)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.410
High resolution limit [Å]	2.350	10.510	2.350
Rmerge	0.064	0.017	0.547
Number of reflections	42603	511	3090
<I/σ(I)>	19.82	54	3.24
Completeness [%]	99.6	88.9	99.9
Redundancy	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	Protein incubated with 4mM each of AMPPnP, halofuginone, B-ME, and MgCl2 for ~5min, then added 1 to 1 with Wiz1/2(a10): 20% PEG-2000 MME, 0.1M Tris base/HCl, pH=7.0, cryoprotected with 20%EG, VAPOR DIFFUSION, SITTING DROP, temperature 289K