1UPI

Mycobacterium tuberculosis rmlC epimerase (Rv3465)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	120
Detector technology	CCD
Collection date	2001-06-15
Detector	ADSC CCD
Spacegroup name	P 32 2 1
Unit cell lengths	64.905, 64.905, 87.203
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.000 - 1.700
R-factor	0.203
Rwork	0.201
R-free	0.24900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dzr
RMSD bond length	0.021 *
RMSD bond angle	1.786 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	EPMR (V. 2.5)
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	55.900	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.052	0.410
Number of reflections	23837	1839 *
<I/σ(I)>	46.82	2.49
Completeness [%]	99.2	93.8
Redundancy	4.4 *	4.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5		0.5 + 0.5 UL SITTING DROPS IN INTELLIPLATES, 0.1 M NA-CITRATE BUFFER, PH 5.5, 46% PEG-MME 2K AND 3 % LDAO B-MERCAPTO-ETHANOL IN PROTEIN STOCK

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	26 (mg/ml)
2	1	reservoir	sodium citrate	0.1 (M)	pH5.5
3	1	reservoir	PEG2000MME	28 (%)
4	1	reservoir	LDAO	0.33 (%)