1S3I

Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-12-02
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54
Spacegroup name	P 21 21 2
Unit cell lengths	100.000, 64.630, 64.590
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.300
R-factor	0.24532
Rwork	0.242
R-free	0.30500 *
Structure solution method	MIR
RMSD bond length	0.010
RMSD bond angle	1.480 *
Data reduction software	CrystalClear ((MSC/RIGAKU))
Data scaling software	d*TREK
Phasing software	PHASES
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.700	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.100	0.346
Total number of observations	80514 *
Number of reflections	19201	1863 *
<I/σ(I)>	5.3	2
Completeness [%]	99.7	100
Redundancy	4.2	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	277	Chumanevich, A.A., (2002) Acta Cryst., D58, 1841. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	1.2-1.4 (M)	pH4.9-5.1
2	1	reservoir	glycerol	5 (%)
3	1	drop	protein	10 (mg/ml)