2WNE

Mutant Laminarinase 16A cyclizes laminariheptaose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-05-16
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	38.175, 47.911, 152.766
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.589 - 2.124
R-factor	0.163
Rwork	0.160
R-free	0.22000
Structure solution method	OTHER
Starting model (for MR)	NONE
RMSD bond length	0.014
RMSD bond angle	1.477
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	REFMAC
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.900	2.200
High resolution limit [Å]	2.110	2.100
Rmerge	0.090	0.240
Number of reflections	16720
<I/σ(I)>	12	5
Completeness [%]	97.0	81
Redundancy	3.6	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5		HANGING DROP: 1 UL 2MG/ML PROTEIN MIXED WITH 1 UL RESERVOIR SOLUTION: 20% PEG 3350, 0.2 M NH4NO3 PH 5 (REERVOIR VOLUME 500 UL). XTALS WERE SOAKED O/N IN DROP OF 10 MM AL7F AND EQUAL VOLUME 35% PEG, 0.2 M NH4NO3 PH 5.