1OJR

L-rhamnulose-1-phosphate aldolase from Escherichia coli (mutant E192A)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-03-15
Detector	MARRESEARCH
Spacegroup name	P 4 21 2
Unit cell lengths	108.024, 108.024, 57.166
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.500 * - 1.350
R-factor	0.112
Rwork	0.111
R-free	0.14200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gt7
RMSD bond length	0.007
RMSD bond angle	1.250 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.500	1.400
High resolution limit [Å]	1.350	1.350
Rmerge	0.052	0.380
Number of reflections	71387	7660 *
<I/σ(I)>	8.7	1.7
Completeness [%]	96.0	95
Redundancy	3.7	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	3 *		HANGING DROP WITH 5 MG/ML PROTEIN AND 18% (V/V) DIOXANE. RESERVOIR WITH 35% (V/V) DIOXANE. HAMPTON CRYSTAL SCREEN-2 NO.4, pH 4.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	potassium phosphate	20 (mM)	pH3.0
2	1	reservoir	dioxane	35 (%(v/v))
3	1	drop	enzyme	10 (mg/ml)