1E5L

Apo saccharopine reductase from Magnaporthe grisea

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-03-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	89.330, 119.000, 195.940
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.910 - 2.400
R-factor	0.222
Rwork	0.222
R-free	0.25900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ff9
RMSD bond length	0.007
RMSD bond angle	23.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.440
High resolution limit [Å]	2.400	2.400
Rmerge	0.090	0.335
Total number of observations	386685 *
Number of reflections	40017
<I/σ(I)>	24	3.3
Completeness [%]	97.1	82.2
Redundancy	9.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4	4 *	8 MG/ML PROTEIN, 11-14 % (W/W) PEG6000, 0.1 M CITRIC ACID PH 4.0, 0.1 % BETA-OCTYLGLUCOSIDE, 1 MM DTT

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	beta-octylglucoside	0.5 (%)
3	1	reservoir	PEG6000	11-14 (%(w/w))
4	1	reservoir	citric acid	0.1 (M)
5	1	reservoir	dithiothreitol	1 (mM)