1JRG

Crystal Structure of the R3 form of Pectate Lyase A, Erwinia chrysanthemi

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	153
Detector technology	IMAGE PLATE
Collection date	2000-04-12
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	H 3
Unit cell lengths	98.055, 98.055, 217.162
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.16
Rwork	0.160
R-free	0.21090 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PelE search model comprised of residues 30-61 70-100 105-251 258-280 293-314 and 323-332. (Coordinates provided by F. Jurnak)
RMSD bond length	0.007
RMSD bond angle	1.418 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.077 *	0.310 *
Total number of observations	111710 *
Number of reflections	44138 *
<I/σ(I)>	12	3.5
Completeness [%]	98.3 *	99.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7	295	PEG 8K, PEG1K, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	10 (mM)	pH7.0
2	1	drop		0.5 (M)
3	1	drop	PEG8000	1 (%)
4	1	reservoir		1 (M)
5	1	reservoir	PEG8000	2 (%)