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Title 

Crystallization and preliminary X-ray analysis of a thermoalkalophilic lipase from Bacillus stearothermophilus L1

Authors 

Seong Tae JeongHyung Kwoun KimSeung Jun KimJae Gu PanTae Kwang OhSeong Eon Ryu

Publisher 

International Union of Crystallography

Issue Date 

2001

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 57, no. 9, pp. 1300-1302

Keywords 

recombinant proteintriacylglycerol lipasecrystallizationgeobacillus stearothermophilusprotein conformationX ray crystallographybacillus stearothermophilusCrystallography, X-RayLipaserecombinant proteins

Abstract 

A thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) was crystallized in two different crystal forms using a low concentration of the enzyme and a calcium-exchange process. The first, needle-like, crystal form, which diffracts to about 3.5 ?, belongs to the orthorhombic space group P212121, with unit-cell parameters a = 67.84, b = 72.96, c = 104.41 ?. The second, monoclinic, crystal form, which behaves better than the first form for crystallographic analyses, belongs to the monoclinic space group C2 and has unit-cell parameters a = 119.62, b = 85.05, c = 98.36 ?, β = 99.73°. From the monoclinic crystals, a native data set and a samarium-derivative data set were collected to 2.0 and 2.3 ? resolution, respectively. The difference Patterson map between the two data sets shows strong heavy-atom peaks, indicating that the crystals are suitable for a high-resolution structure determination.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 57(9): 1300-1302

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S0907444901010332

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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