1JEO

Crystal Structure of the Hypothetical Protein MJ1247 from Methanococcus jannaschii at 2.0 A Resolution Infers a Molecular Function of 3-Hexulose-6-Phosphate isomerase.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	280
Detector technology	IMAGE PLATE
Collection date	1999-09-15
Detector	RIGAKU RAXIS II
Wavelength(s)	1.5418
Spacegroup name	I 2 2 2
Unit cell lengths	67.921, 68.155, 83.336
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.1891 *
Rwork	0.189
R-free	0.22650
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MJ1247 model obtained from MAD data (selenomethionine-derivatized crystals)
RMSD bond length	0.013
RMSD bond angle	1.393
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.080 *	0.320
Total number of observations	37198 *
Number of reflections	12655 *
<I/σ(I)>	11.5	1.98
Completeness [%]	94.0 *	75.5 *
Redundancy	4.44	1.63

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	22 *	40% PEG 400, 0.1 M Tris/HCl, 0.2 M Sodium citrate, 10 mM betamercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	40 (%)
2	1	reservoir	Tris-HCl	0.1 (M)	pH8.5
3	1	reservoir	sodium citrate	0.2 (M)
4	1	reservoir	beta-mercaptoethanol	10 (mM)