1RTW

X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	2003-09-12
Detector	BRANDEIS - B4
Wavelength(s)	0.979, 0.9794, 0.95
Spacegroup name	P 21 21 2
Unit cell lengths	101.800, 123.650, 77.470
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.350
Rwork	0.240
R-free	0.28000 *
Structure solution method	MAD
RMSD bond length	0.007 *
RMSD bond angle	1.100 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.380
High resolution limit [Å]	2.350	2.350
Rmerge	0.070 *	0.330 *
Total number of observations	239958 *
Number of reflections	73637 *	6861 *
<I/σ(I)>	18.7	3.7
Completeness [%]	93.5 *	89.7 *
Redundancy	3.3 *	3.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	277	20% PEG400, 200mM CaCl2, 50mM cacodylic acid, 1mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	20 (%)
2	1	reservoir		200 (mM)
3	1	reservoir	dithiothreitol	1 (mM)
4	1	reservoir	cacodylate	50 (mM)	pH7.5
5	1	drop	protein	8 (mg/ml)
6	1	drop	Tris	10 (mM)
7	1	drop		100 (mM)
8	1	drop	dithiothreitol	5 (mM)	pH8.0