1GZG

Complex of a Mg2-dependent porphobilinogen synthase from Pseudomonas aeruginosa (mutant D139N) with 5-fluorolevulinic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-10-15
Detector	MARRESEARCH
Spacegroup name	P 4 21 2
Unit cell lengths	127.131, 127.131, 86.145
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	91.300 * - 1.660
Rwork	0.175
R-free	0.19800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1b4k
RMSD bond length	0.020 *
RMSD bond angle	1.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.0.32)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.720
High resolution limit [Å]	1.660	1.660
Rmerge	0.116	0.394
Total number of observations	433947 *
Number of reflections	82775
<I/σ(I)>	11	4.1
Completeness [%]	99.9	100
Redundancy	5.2	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sparse matrix screening *	7.5 *		PROTEIN SOLUTION: 12 MG/ML PBGS MUTANT D139N IN 50 MM K-HEPES, 10 MM MGCL2. CRYSTALLIZATION SOLUTION: 0.99 ML PROTEIN SOLUTION = 0.01 ML 2MM 5F-LA IN 50 MM K-HEPES, 10 MM MGCL2. RESERVOIR SOLUTION: 1 M NA/K-TARTRATE, 0.2M LI2SO4, 0.1 M CHES PH = 9,5. SITTING DROP: 0.003 ML CRYSTALLISATION SOLUTION + 0.003 ML RESERVOIR SOLUTION

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	potassium-HEPES	50 (mM)	pH7.5
2	1	1		10 (mM)
3	1	1	protein	12 (mg/ml)
4	1	1	5F-LA	2 (mM)
5	1	2	glycerol	30 (%(v/v))