1M5S

Formylmethanofuran:tetrahydromethanopterin fromyltransferase from Methanosarcina barkeri

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	127.100, 83.800, 126.400
Unit cell angles	90.00, 108.40, 90.00

Refinement procedure

Resolution	30.000 * - 1.900 *
R-factor	0.197
Rwork	0.197
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Formylmethanofuran:tetrahydromethanopterin formyltransferase from Methanopyrus kandleri
RMSD bond length	0.007
RMSD bond angle	26.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.3)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.920
High resolution limit [Å]	1.900 *	1.880 *
Rmerge	0.037 *	0.081 *
Total number of observations	215926 *
Number of reflections	99960
Completeness [%]	94.0	84.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	MPD, sodium citrate, ammonium acetate, HEPES, formylmethanofuran, pH 6.7, VAPOR DIFFUSION, HANGING DROP at 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	MOPS	10 (mM)	pH7.0
3	1	reservoir	sodium citrate	0.1 (M)
4	1	reservoir	ammonium acetate	0.2 (M)
5	1	reservoir	MPD	31 (%)
6	1	reservoir	HEPES	0.1 (M)	pH6.7
7	1	reservoir	formylmethanofuran	5.0 (mM)