1V7R

Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-11-12
Detector	RIGAKU RAXIS
Wavelength(s)	1.0
Spacegroup name	C 2 2 21
Unit cell lengths	79.013, 93.188, 55.621
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.000 * - 1.400
R-factor	0.202
Rwork	0.202
R-free	0.22200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1b78
RMSD bond length	0.004 *
RMSD bond angle	1.150 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	1.450
High resolution limit [Å]	1.400	1.400
Rmerge	0.050	0.272 *
Total number of observations	286969 *
Number of reflections	40686 *
Completeness [%]	99.8 *	100
Redundancy	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	5.1	291 *	1.6M Tris sodium citrate, pH 5.1, Microbatch, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20.4 (mg/ml)
2	1	reservoir	sodium citrate	1.6 (M)	pH5.1