1O22

Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00 A resolution

Experimental procedure

Experimental method	MAD
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	2002-10-13
Detector	ADSC QUANTUM
Wavelength(s)	0.97780, 0.91840, 0.97920
Spacegroup name	P 43 21 2
Unit cell lengths	58.410, 58.410, 102.490
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.160 * - 2.000
R-factor	0.186
Rwork	0.182
R-free	0.23800
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	1.440 *
Data reduction software	XFIT
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.160 *	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.061 *	0.375 *
Total number of observations	148070 *
Number of reflections	12462
<I/σ(I)>	28.1	3.2
Completeness [%]	99.0	90.9
Redundancy	11.8	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.9 *	293	25.5 % PEG 4000; 0.085 M Tris pH 8.5; 0.17 M Na(Ac), 15 % Glycerol, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K, pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris	20 (mM)	pH7.9
2	1	drop		150 (mM)
3	1	drop	TCEP	0.25 (mM)
4	1	drop	protein	9.4 (mg/ml)
5	1	reservoir	PEG4000	25.5 (%)
6	1	reservoir	Tris	0.085 (M)	pH8.5
7	1	reservoir	sodium acetate	0.17 (M)
8	1	reservoir	glycerol	15 (%)