1WDE

Crystal structure of the conserved hypothetical protein APE0931 from Aeropyrum pernix K1

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-04-16
Detector	RIGAKU JUPITER 210
Wavelength(s)	0.97909, 0.97940, 0.96400
Spacegroup name	P 41 21 2
Unit cell lengths	62.827, 62.827, 129.728
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.530 - 2.000
R-factor	0.199
Rwork	0.199
R-free	0.24400
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.700
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Number of reflections	18308
<I/σ(I)>	20.07	7.471
Completeness [%]	99.7	100
Redundancy	7.697

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	293	30% MPD, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K