2E7F

5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 Angsrom resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-07-30
Detector	BRANDEIS - B4
Wavelength(s)	0.91938
Spacegroup name	P 21 21 21
Unit cell lengths	50.159, 78.547, 135.617
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.880 - 2.200
R-factor	0.178
Rwork	0.172
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f6y
RMSD bond length	0.006
RMSD bond angle	1.018
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	EPMR
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.920	2.260
High resolution limit [Å]	2.200	2.200
Rmerge	0.086
Number of reflections	26806
<I/σ(I)>	11.5	3.5
Completeness [%]	96.2	87.9
Redundancy	3.8	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	8-15% PEGmme 5000, 0.05M Calcium acetate, 20% Glycerol, 0.05M HEPES buffer; 3-fold molar excess of the MTHF substrate (Schricks Labolatories, Jona, Switzerland). The supersaturation of the precipitant solution required dilution of the protein-CH3-H4folate complex by 50-100-fold in order to obtain single crystals., pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K