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Digitale Medien

Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II (1994)

Liu, Rui-Qin ; Miller, Mark A. ; Han, Gye Won ; [weitere]

s.l. : American Chemical Society

Biochemistry 33 (1994), S. 8678-8685

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ISSN: 1520-4995

Quelle: ACS Legacy Archives

Thema: Biologie , Chemie und Pharmazie

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1021/bi00195a008

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Digitale Medien

Lactate dehydrogenase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray analysis (2000)

Lee, Byung Il ; Chang, Changsoo ; Cho, Seung Je ; [weitere]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 56 (2000), S. 81-83

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ISSN: 1399-0047

Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik

Notizen: L(+)-Lactate dehydrogenase (LDH) is a key enzyme in anaerobic metabolism which converts pyruvate to lactate. LDH from the hyperthermophilic archaebacterium Methanococcus jannaschii has been overexpressed in Escherichia coli and crystallized in two crystal forms at 297 K using 2-methyl-2,4-pentanediol as precipitant. Type I crystals grew rapidly and diffracted to at least 2.8 Å Bragg spacing upon exposure to Cu Kα X-rays. X-ray diffraction data to 2.9 Å have been collected from a native crystal. The type I crystal is tetragonal, belonging to the space group P42212, with unit-cell parameters a = b = 99.74, c = 170.00 Å. The asymmetric unit contains two LDH subunits, with a corresponding crystal volume per protein mass (Vm) of 3.05 Å3 Da−1 and a solvent content of 59.7%. Type II crystals, which grew more slowly, diffracted to at least 1.8 Å Bragg spacing upon exposure to Cu Kα X-rays. X-ray diffraction data to 1.9 Å have been collected from a native crystal. The type II crystal is orthorhombic, belonging to the space group P21212, with unit-cell parameters a = 47.65, b = 125.10, c = 58.08 Å. The asymmetric unit contains a single LDH subunit, with a corresponding crystal volume per protein mass (Vm) of 2.50 Å3 Da−1 and a solvent content of 50.8%. Therefore, the type II crystal is more suitable for high-resolution structure determination than the type I crystal.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1107/S090744499901389X

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Direct-methods determination of an RNA/DNA hybrid decamer at 1.15 Å resolution (2001)

Han, Gye Won

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 57 (2001), S. 213-218

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ISSN: 1399-0047

Quelle: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Thema: Chemie und Pharmazie , Geologie und Paläontologie , Physik

Notizen: For the first time, ab initio direct methods have been used to solve the crystal structure of an RNA/DNA hybrid decamer. The RNA/DNA sequence corresponds to the leftmost two-thirds of the polypurine tract (PPT), the primer for second-strand DNA synthesis by HIV-1 reverse transcriptase (RT). Direct methods using Shake-and-Bake (SnB) yielded solutions for the RNA/DNA decamer molecule using 1.15 Å data, which is just on the resolution edge of what might work with direct methods. Atomic positions for 96% of the entire molecule, containing 514 non-H atoms including three Ca2+ ions, were easily interpreted from a Fourier map based on the `Shake-and-Bake' minimal function and CROQUE phase-refinement program. Only six atoms, primarily in the sugar linkage, were missing in this Fourier map. At present, the R factor of the model is 0.143 (Rfree = 0.186) for the 562 non-H atom sites located. The conformation of the RNA/DNA helix is A-form, with a typical A-helix minor-groove width. This paper presents the methodology used in solving this structure.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1107/S0907444900017595

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