1R67

Y104A MUTANT OF E.COLI IPP ISOMERASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2003-04-11
Detector	MARRESEARCH
Wavelength(s)	0.9798
Spacegroup name	P 32 2 1
Unit cell lengths	71.648, 71.648, 61.327
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 * - 1.760 *
R-factor	0.1967
Rwork	0.190
R-free	0.23560 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hzt
RMSD bond length	0.006
RMSD bond angle	0.023
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELX
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	1.800
High resolution limit [Å]	1.760 *	1.760 *
Rmerge	0.040	0.169 *
Total number of observations	31357 *
Number of reflections	16594 *
Completeness [%]	89.9	93.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	20 *	PEG 2000, MANGANESE CHLORIDE, MAGNESIUM CHLORIDE, AMMONIUM SULFATE, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 275K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.0 (mg/ml)
2	1	reservoir	PEG2000 MME	10-16 (%(w/v))	pH4.5-6.5