Purification, crystallization and preliminary crystallographic analysis of the putative thiamine-biosynthesis protein PH1313 from Pyrococcus horikoshii OT3

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106054509· OSTI ID:22360252

Sugahara, Michihiro; Murai, Satoko ^[1]; Sugahara, Mitsuaki ^[2]; Kunishima, Naoki ^[1]

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1. Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148 (Japan)
2. Structural Biophysics Laboratory, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148 (Japan)

The putative thiamine-biosynthesis protein PH1313 from P. horikoshii OT3 was overexpressed, purified and crystallized. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1} and diffract X-rays to 1.9 Å resolution. The putative thiamine-biosynthesis protein PH1313 from Pyrococcus horikoshii OT3 has been overexpressed and purified. Crystallization was performed by the oil-microbatch method using 28%(v/v) 2-methyl-2,4-pentanediol as a precipitant at 291 K. A native X-ray diffraction data set at 1.9 Å resolution and a single anomalous dispersion data set from a selenomethionine-derivative crystal at 2.1 Å resolution were collected using synchrotron radiation at 100 K. The native crystal belongs to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 71.7, b = 71.2, c = 141.8 Å.

• OSTI ID: 22360252
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DISPERSIONS
PROTEINS
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION