1LFP

Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2002-03-05
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97864
Spacegroup name	P 21 21 21
Unit cell lengths	43.790, 65.350, 73.780
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.710 *
R-factor	0.228 *
Rwork	0.228
R-free	0.29400
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.560 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.200	1.730
High resolution limit [Å]	1.710 *	1.710 *
Rmerge	0.051 *	0.207 *
Number of reflections	42899 *	1081 *
Completeness [%]	96.0 *	48.2 *
Redundancy	7.5 *	5.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.8	21.5-22.5 *	20% PEG3350, 0.2M Ammonium Nitrate, 10 mM NAD, 3% PEG400, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	Tris-HCl	25 (mM)	pH6.8
3	1	drop		110 (mM)
4	1	drop	PEG3350	10 (%)
5	1	drop	ammonium nitrate	0.1 (M)
6	1	drop	NAD	5 (mM)
7	1	drop	PEG400	1.5 (%)
8	1	reservoir	PEG3350	20 (%)
9	1	reservoir	ammonium nitrate	0.2 (M)