3REQ

METHYLMALONYL-COA MUTASE, SUBSTRATE-FREE STATE (POOR QUALITY STRUCTURE)

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-06
Detector	MAR scanner 300 mm plate
Spacegroup name	P 41 21 2
Unit cell lengths	110.910, 110.910, 257.740
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.313 *
Rwork	0.313
R-free	0.39300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2req
RMSD bond length	0.012
RMSD bond angle	0.046
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.000	2.850
High resolution limit [Å]	2.700	2.700
Rmerge	0.072	0.381
Number of reflections	44606
<I/σ(I)>	7.9	2
Completeness [%]	99.2	99.2 *
Redundancy	9	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5		PROTEIN SOLUTION: 20 MG/ML PROTEIN, 1MM ADENOSYLCOBALAMIN, 1MM DTT, TRIS PH 7.5. RESERVOIR: 14% PEG 4000 (W/V), 20% GLYCEROL (V/V), 100MM TRIS-HCL PH 7.5. EQUAL VOLUMES OF PROTEIN SOLUTION AND RESERVOIR MIXED, AND EQUILIBRATED BY VAPOR DIFFUSION., vapor diffusion

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	PEG	14 (%)