1RO0

Bifunctional DNA primase/polymerase domain of ORF904 from the archaeal plasmid pRN1- Triple mutant F50M/L107M/L110M SeMet remote

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-29
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9793, 0.9797, 1.28
Spacegroup name	P 21 21 2
Unit cell lengths	47.532, 119.424, 41.943
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.800
Rwork	0.232
R-free	0.24300 *
Structure solution method	MAD
RMSD bond length	0.006 *
RMSD bond angle	1.220 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.053	0.322
Number of reflections	22672	2225 *
Completeness [%]	99.2	99.6
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	20 *	Tris, sodium acetate, PEG 4000, DTT, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-Cl	100 (mM)	pH8.5
2	1	reservoir	sodium acetate	200 (mM)
3	1	reservoir	PEG4000	30 (%(w/v))
4	1	reservoir	dithiothreitol	5 (mM)
5	1	drop	HEPES	10 (mM)	pH7.5
6	1	drop		150 (mM)
7	1	drop	dithiothreitol	3 (mM)
8	1	drop	protein	25 (mg/ml)