3ERJ

Crystal structure of the peptidyl-tRNA hydrolase AF2095 from Archaeglobus fulgidis. Northeast Structural Genomics Consortium target GR4

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4C
Synchrotron site	NSLS
Beamline	X4C
Temperature [K]	100
Detector technology	CCD
Collection date	2008-09-30
Detector	MAR CCD 165 mm
Wavelength(s)	0.97877
Spacegroup name	P 21 21 21
Unit cell lengths	43.903, 46.925, 105.263
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.880 - 1.800
R-factor	0.195
Rwork	0.195
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rlk
RMSD bond length	0.005
RMSD bond angle	1.100
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.055	0.282
Number of reflections	38783
<I/σ(I)>	34.46	4.45
Completeness [%]	99.6	97.5
Redundancy	7.2	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	291	Protein solution: 10 mM Tris (pH 7.5), 100 mM sodium chloride, and 5 mM DTT. Reservoir solution: 100 mM Tris (pH 8), 20% PEG3350, 200 mM NaCl, and 0.5% w/v polyvinylpyrrolidone K15 , VAPOR DIFFUSION, SITTING DROP, temperature 291K