1P9L

Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1996-09-12
Detector	SIEMENS
Wavelength(s)	1.5418
Spacegroup name	I 21 21 21
Unit cell lengths	119.290, 117.280, 78.540
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 2.300
R-factor	0.197
Rwork	0.193
R-free	0.25000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1arz
RMSD bond length	0.011
RMSD bond angle	26.900 *
Data reduction software	SAINT
Data scaling software	SAINT
Phasing software	AMoRE
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.400
High resolution limit [Å]	2.300	2.300
Rmerge	0.078 *	0.206 *
Total number of observations	77959 *
Number of reflections	24502	2353 *
<I/σ(I)>	13.6	3.3
Completeness [%]	98.5	95.1
Redundancy	3.2	2.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	ammonium Sulfate, PEG 400, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	NADH	2 (mM)
3	1	drop	2,6-PDC	30 (mM)
4	1	reservoir	ammonium sulfate	2.2 (M)
5	1	reservoir	HEPES	0.1 (M)	pH7.5
6	1	reservoir	PEG400	3 (%)