1H42

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR AND LEU 263 REPLACED BY PRO (T155G-A160T-L263P)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-11-15
Detector	MAR scanner 180 mm plate
Spacegroup name	P 65
Unit cell lengths	85.810, 85.810, 96.130
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	14.860 - 2.150
R-factor	0.2
Rwork	0.200
R-free	0.23100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1que
RMSD bond length	0.018
RMSD bond angle	27.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.940 *	2.270
High resolution limit [Å]	2.150	2.150
Rmerge	0.095	0.287
Number of reflections	21605 *
<I/σ(I)>	0.095	0.287
Completeness [%]	98.9	98.9
Redundancy	6.6	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *	20 *	pH 5.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	10 (mM)	pH8.0
2	1	drop	beta-octylglucoside	5 (%(w/v))
3	1	reservoir	PEG6000	18-20 (%(w/v))
4	1	reservoir	ammonium sulfate	20 (mM)
5	1	reservoir	MES-NaOH	0.1 (M)	pH5.0