1SU5

Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	CCD
Collection date	2001-05-27
Detector	MARRESEARCH
Wavelength(s)	0.8
Spacegroup name	P 41 21 2
Unit cell lengths	86.756, 86.756, 163.376
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.790 - 2.700
R-factor	0.18726
Rwork	0.185
R-free	0.23638
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	8tim
RMSD bond length	0.012
RMSD bond angle	1.235
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.690
High resolution limit [Å]	2.600	2.590
Rmerge	0.109	0.392
Number of reflections	19906
<I/σ(I)>	16.5	5.2
Completeness [%]	99.0	97.5
Redundancy	8.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	294	Citrate, ammonium sulphate, sodium chloride, 2-phosphoglycolate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K