1OOC

Mutations in the T1.5 loop of pectate lyase A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	153
Detector technology	IMAGE PLATE
Collection date	2003-01-24
Detector	MAR scanner 300 mm plate
Spacegroup name	P 21 21 2
Unit cell lengths	94.758, 151.205, 50.897
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.900 *
R-factor	0.219
Rwork	0.219
R-free	0.27480 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1JTA with out residues 215-226
RMSD bond length	0.008
RMSD bond angle	1.570 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.080
High resolution limit [Å]	2.900	2.900
Rmerge	0.097 *	0.273 *
Total number of observations	128721 *
Number of reflections	14754
<I/σ(I)>	23.6	14.6
Completeness [%]	91.6	81
Redundancy	8.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	295 *	PEG 5000 monomethyl ether (MME), 0.1M MES (2-[N-Morpholino]ethanesulfonic acid), pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000 MME	17.6-20 (%)
2	1	reservoir	MES	0.1 (M)	pH6.5
3	1	drop	protein	8.72 (mg/ml)
4	1	drop	PEG5000 MME	2.9-3.3 (%)
5	1	drop	MES	0.02 (M)	pH6.5