Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase

Citation
M. Akita et al., Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase, ACT CRYST D, 56, 2000, pp. 749-750
Citations number
11
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
6
Pages
749 - 750
Database
ISI
SICI code
0907-4449(200006)56:<749:CAPXAO>2.0.ZU;2-O
Abstract
Pel-15, a high-alkaline pectate lyase (pectate transeliminase; E.C. 4.2.2.2 ) from Bacillus sp. strain KSM-P15, has been crystallized using the hanging -drop vapour-diffusion method at 277 K. Two different crystal forms were ob tained and preliminary X-ray diffraction data were collected from each crys tal form at 100 K. Both forms belong to the orthorhombic space group P2(1)2 (1)2(1) and contain one molecule per asymmetric unit. The unit-cell paramet ers of form I are a = 43.2 (2), b = 60.2 (2), c = 82.2 (2) Angstrom and tho se of form II are a = 42.9 (1), b = 43.4 (1), c = 105.9 (3) Angstrom. Diffr action data to a resolution of 1.5 Angstrom were collected from form II cry stals using a synchrotron-radiation source.