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26 results on '"Chrzas, John"'

5. High-resolution crystal structures of recombinant wild-type and selenomethione-labeled bovine trypsin (S195A) mutant reveals no electron density for three surface loops that includes the C191–C220 disulfide

Author

Rose, John, primary, Zhou, Dayong, additional, Fu, Zheng-Qing Albert, additional, Jin, Zhongmin, additional, Gonczy, John, additional, Chrzas, John, additional, Kandavelu, Palani, additional, Salazar, Rodrick, additional, Gul, Maaz, additional, Chen, Lirong, additional, Wang, Bi-Cheng, additional, and Chinte, Unmesh, additional

Published
2020
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7. UGA-APS soft X-ray pilot program at SER-CAT 22BM: Phase II – chromatic exploration of uncharted aspects of metals in macromolecules

Author

Wang, Bi-Cheng, primary, Rose, John, additional, Chrzas, John, additional, Chen, Lirong, additional, Kandavelu, Palani, additional, Zhou, Dayong, additional, Chinte, Unmesh, additional, Fu, Zheng-Qing, additional, Jin, Zhongmin, additional, Fait, James, additional, Rosenbaum, Gerold, additional, and Mills, Dennis, additional

Published
2017
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8. Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschii

Author

Watanabe, Yuzo, primary, Yanai, Hisaaki, additional, Kanagawa, Mayumi, additional, Suzuki, Sakiko, additional, Tamura, Satoko, additional, Okada, Kiyoshi, additional, Baba, Seiki, additional, Kumasaka, Takashi, additional, Agari, Yoshihiro, additional, Chen, Lirong, additional, Fu, Zheng-Qing, additional, Chrzas, John, additional, Wang, Bi-Cheng, additional, Nakagawa, Noriko, additional, Ebihara, Akio, additional, Masui, Ryoji, additional, Kuramitsu, Seiki, additional, Yokoyama, Shigeyuki, additional, Sampei, Gen-ichi, additional, and Kawai, Gota, additional

Published
2016
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10. SER-CAT Light When YOU Need It via automation & remote access

Author

Rose, John, primary, Chrzas, John, additional, Fait, Jim, additional, Gonczy, John, additional, Fu, "Zheng-Qing ""Albert""", additional, Jin, Zhongmin, additional, Salazar, Rod, additional, Chinte, Unmesh, additional, Kandavelu, Palani, additional, and Wang, Bi-Cheng, additional

Published
2014
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11. Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii.

Author

Watanabe, Yuzo, Yanai, Hisaaki, Kanagawa, Mayumi, Suzuki, Sakiko, Tamura, Satoko, Okada, Kiyoshi, Baba, Seiki, Kumasaka, Takashi, Agari, Yoshihiro, Chen, Lirong, Fu, Zheng-Qing, Chrzas, John, Wang, Bi-Cheng, Nakagawa, Noriko, Ebihara, Akio, Masui, Ryoji, Kuramitsu, Seiki, Yokoyama, Shigeyuki, Sampei, Gen-ichi, and Kawai, Gota

Subjects
CRYSTAL structure, ENZYMES, METHANOCALDOCOCCUS jannaschii
Abstract

The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular-dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion. [ABSTRACT FROM AUTHOR]

Published
2016
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13. Structure of the human Tim44 C-terminal domain in complex with pentaethylene glycol: ligand-bound form

Author

Handa, Noriko, primary, Kishishita, Seiichiro, additional, Morita, Satoshi, additional, Akasaka, Ryogo, additional, Jin, Zhongmin, additional, Chrzas, John, additional, Chen, Lirong, additional, Liu, Zhi-Jie, additional, Wang, Bi-Cheng, additional, Sugano, Sumio, additional, Tanaka, Akiko, additional, Terada, Takaho, additional, Shirouzu, Mikako, additional, and Yokoyama, Shigeyuki, additional

Published
2007
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15. A robust cryogenic crystal design in use at the APS.

Author

Ivanov, Ivan, Rosenbaum, Gerd, Chrzas, John, Fischetti, Robert, Segre, C. U., and Chapman, L. D.

Subjects
SILICON crystals, LOW temperature engineering, SYNCHROTRON radiation sources
Abstract

A simple and robust design for the liquid nitrogen-cooled first monochromator crystal suitable for large Bragg-angles has been implemented at three undulator beamlines at the Advanced Photon Source (IMCA CAT, BioCAT, and MR CAT). The design features a simple and reliable seal and a strain free mount. The system has been pressure tested intentionally and accidentally to failure and the crystal reseals. Measurements have been made under closed gap conditions with little indication of distortion. The crystal design, implementation and measurements are presented. © 2000 American Institute of Physics. [ABSTRACT FROM AUTHOR]

Published
2000

21. Structure of the Archaeoglobus fulgidus orphan ORF AF1382 determined by sulfur SAD from a moderately diffracting crystal.

Author

Zhu, Jin-Yi, Fu, Zheng-Qing, Chen, Lirong, Xu, Hao, Chrzas, John, Rose, John, and Wang, Bi-Cheng

Subjects
CRYSTAL structure, ARCHAEOGLOBUS fulgidus, SULFUR, SYNCHROTRON radiation, STRUCTURAL genomics, X-ray diffraction, CYSTEINE
Abstract

The crystal structure of the 11.14 kDa orphan ORF 1382 from Archaeoglobus fulgidus (AF1382) has been determined by sulfur SAD phasing using a moderately diffracting crystal and 1.9 Å wavelength synchrotron X-rays. AF1382 was selected as a structural genomics target by the Southeast Collaboratory for Structural Genomics (SECSG) since sequence analyses showed that it did not belong to the Pfam-A database and thus could represent a novel fold. The structure was determined by exploiting longer wavelength X-rays and data redundancy to increase the anomalous signal in the data. AF1382 is a 95-residue protein containing five S atoms associated with four methionine residues and a single cysteine residue that yields a calculated Bijvoet ratio (Δ Fanom/ F) of 1.39% for 1.9 Å wavelength X-rays. Coupled with an average Bijvoet redundancy of 25 (two 360° data sets), this produced an excellent electron-density map that allowed 69 of the 95 residues to be automatically fitted. The S-SAD model was then manually completed and refined ( R = 23.2%, Rfree = 26.8%) to 2.3 Å resolution (PDB entry 3o3k). High-resolution data were subsequently collected from a better diffracting crystal using 0.97 Å wavelength synchrotron X-rays and the S-SAD model was refined ( R = 17.9%, Rfree = 21.4%) to 1.85 Å resolution (PDB entry 3ov8). AF1382 has a winged-helix-turn-helix structure common to many DNA-binding proteins and most closely resembles the N-terminal domain (residues 1-82) of the Rio2 kinase from A. fulgidus, which has been shown to bind DNA, and a number of MarR-family transcriptional regulators, suggesting a similar DNA-binding function for AF1382. The analysis also points out the advantage gained from carrying out data reduction and structure determination on-site while the crystal is still available for further data collection. [ABSTRACT FROM AUTHOR]

Published
2012
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26. A parallel program using SHELXD for quick heavy-atom partial structural solution on high-performance computers.

Author

Fu, Zheng-Qing, Chrzas, John, Sheldrick, George M., Rose, John, and Wang, Bi-Cheng

Subjects
*COMPUTER software, *PARALLEL algorithms, *CRYSTALLOGRAPHY, *PARALLEL computers, *SYNCHROTRONS, *LINUX operating systems
Abstract

A parallel algorithm has been designed for SHELXD to solve the heavy-atom partial structures of protein crystals quickly. Based on this algorithm, a program has been developed to run on high-performance multiple-CPU Linux PCs, workstations or clusters. Tests on the 32-CPU Linux cluster at SER-CAT, APS, Argonne National Laboratory, show that the parallelization dramatically speeds up the process by a factor of roughly the number of CPUs applied, leading to reliable and instant heavy-atom sites solution, which provides the practical opportunity to employ heavy-atom search as an alternative tool for anomalous scattering data quality evaluation during single/multiple-wavelength anomalous diffraction (SAD/MAD) data collection at synchrotron beamlines. [ABSTRACT FROM AUTHOR]

Published
2007
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