1P5H

Crystal structure of Formyl-CoA Transferase (apoenzyme) from Oxalobacter formigenes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	110
Detector technology	CCD
Collection date	2001-12-09
Detector	ADSC QUANTUM 4
Wavelength(s)	0.933
Spacegroup name	I 4
Unit cell lengths	151.440, 151.440, 99.490
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 * - 2.200
R-factor	0.17295
Rwork	0.171
R-free	0.20900 *
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.297
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SOLVE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.098 *	0.236 *
Number of reflections	57045 *
<I/σ(I)>	15.3	4.9
Completeness [%]	99.0 *	99
Redundancy	5.1	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291 *	Ricagno, S., (2003) Acta Crystallogr., D59, 1276. *
1	VAPOR DIFFUSION, HANGING DROP	7.5	291 *	Ricagno, S., (2003) Acta Crystallogr., D59, 1276. *
1	VAPOR DIFFUSION, HANGING DROP	7.5	291 *	Ricagno, S., (2003) Acta Crystallogr., D59, 1276. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	reservoir	PEG4000	26 (%)
3	1	reservoir	HEPES	100 (mM)	pH7.5
4	1	reservoir		0.5 (M)