2WLQ

Nucleophile-disabled Lam16A mutant holds laminariheptaose (L7) in a cyclical conformation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-3
Synchrotron site	MAX II
Beamline	I911-3
Temperature [K]	100
Detector technology	CCD
Collection date	2006-09-13
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	38.273, 47.910, 152.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	23.843 - 1.400
R-factor	0.171
Rwork	0.170
R-free	0.19400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cl2
RMSD bond length	0.012
RMSD bond angle	1.615
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SCALA
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.800	1.480
High resolution limit [Å]	1.400	1.400
Rmerge	0.080	0.400
Number of reflections	56288
<I/σ(I)>	16.6	3.3
Completeness [%]	98.2	99.2
Redundancy	6.3	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5	293	8 MG/ML PROTEIN SOLUTION IN 10 MM NAOAC WAS MIXED WITH AN EQUAL VOLUME OF CRYSTALLIZATION BUFFER CONTAINING 20% PEG 3350, 0.2 M AMMONIUM NITRATE AND 10 MM SODIUM ACETATE BUFFER, PH 5.0, AT 20 DEGREES. SOAKING: 24 H IN 5 MM LAMINAROHEPTASACCHARIDE. CRYOPROTECTANT CONTAINED 35 % (W/V) PEG 3350, 0.2 M AMMONIUM NITRATE AND 10 MM SODIUM ACETATE BUFFER, PH 5.0