2J40

1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound inhibitor L-proline and NAD.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-24
Detector	RIGAKU CCD
Spacegroup name	H 3
Unit cell lengths	102.043, 102.043, 278.600
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.100
R-factor	0.142
Rwork	0.140
R-free	0.18900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bjk
RMSD bond length	0.017
RMSD bond angle	1.536
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	REFMAC (5)
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.100	0.320
Number of reflections	62989
<I/σ(I)>	11.1	2
Completeness [%]	99.7	98.9
Redundancy	3.2	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.2		PROTEIN WAS CRYSTALLIZED FROM 37.5% MRD, 50 MM SODIUM CITRATE, PH 5.2; THEN SOAKED IN 2MM NAD, 100MM L-PROLINE, 50 MM SODIUM ACETATE PH5.2.