3NFY

The Structure of Human Bisphosphoglycerate Mutase to 1.94A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2006-09-03
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.4
Spacegroup name	P 1 21 1
Unit cell lengths	38.472, 61.345, 122.696
Unit cell angles	90.00, 95.87, 90.00

Refinement procedure

Resolution	54.810 - 1.940
R-factor	0.183
Rwork	0.178
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1T8P.pdb
RMSD bond length	0.022
RMSD bond angle	1.882
Data reduction software	MOSFLM
Data scaling software	SCALA (3.2.17)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	122.169	54.830	2.040
High resolution limit [Å]	1.940	6.130	1.940
Rmerge	0.062	0.032	0.281
Total number of observations		5016	17704
Number of reflections	40132
<I/σ(I)>	15.4	16.5	2
Completeness [%]	95.0	98.8	84.9
Redundancy	3.6	3.6	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	290	20% PEG 6K, 100mM Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K