2BM6

The Structure of MfpA (Rv3361c, C2221 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	93
Detector technology	IMAGE PLATE
Detector	MSC RAXIS IV
Spacegroup name	C 2 2 21
Unit cell lengths	33.393, 48.573, 188.367
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.200
R-factor	0.197
Rwork	0.197
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PREVIOUS STRUCTURE DETERMINED BY SE-MET MAD
RMSD bond length	0.020
RMSD bond angle	1.920
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.060	0.140
Number of reflections	8004
<I/σ(I)>	27.7	8
Completeness [%]	97.1	92.3
Redundancy	6.4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.5		PROTEIN (10 MG/ML, 10 MM AMMONIUM CITRATE PH 7.5, 30 MM BETA-MERCAPTOETHANOL) CRYSTALLIZED IN 35% 2-ETHOXYETHANOL, 100 MM CITRATE PH 5.5. CRYSTAL WAS SOAKED IN 100 MM MES PH 5.2, 30 % PEG400, 1 M CESIUM CHLORIDE PRIOR TO VITRIFICATION AND DATA COLLECTION.