1L5X

The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	105
Detector technology	CCD
Collection date	2002-01-18
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97870, 0.97860, 0.96485
Spacegroup name	P 31 2 1
Unit cell lengths	90.500, 90.500, 129.951
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 * - 2.000
Rwork	0.185
R-free	0.22300
Structure solution method	MAD
RMSD bond length	0.014
RMSD bond angle	1.790 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.099	0.781
Total number of observations	297069 *
Number of reflections	42129
<I/σ(I)>	17.4	2.5
Completeness [%]	99.9	100
Redundancy	7.1	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.55	19.8 *	PEG 4000, sodium acetate, glycerol, Tris buffer, pH 8.55, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11.4 (mg/ml)
2	1	reservoir	Tris	0.083 (M)	pH8.55
3	1	reservoir	PEG4000	21.7 (%(v/v))
4	1	reservoir	sodium acetate	0.17 (M)
5	1	reservoir	glycerol	15 (%(v/v))