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Open Access Publications from the University of California

Scholarly Works (5 results)

  • Article
LBL Publications (2004)

The Control System for the Advanced Light Source uses in-house designed IndustryPack (IP) I/O Modules in compact PCI (cPCI) chassis to control instrumentation. Each module consists of digital I/O ports and 16-bit analog I/O interfaced to instrumentation via a cPCI rear I/O card. During the past few years of installed operation, several factors have prompted investigation into the design of a new IP I/O Module. The ADC channels have significant offset drift over periods of days of initial installed operation. An in-situ calibration procedure was developed to address this problem, but it lacks speed and is inconvenient to perform. Digital I/O port limitations have led to increasing amounts of wasted I/O. Fast orbit feedback requires faster ADC sampling and better filtering than the current IP module offers. This paper discusses the issues related to the current IP I/O Module and the design of a new Double-size IP I/O Module.

    Cover page: ALS control system IP I/O module upgrade
    • Article
    LBL Publications (2002)

    The Control System for the Advanced Light Source (ALS) at Lawrence Berkeley National Lab (LBNL) uses in-house designed IndustryPack(registered trademark) (IP) modules contained in compact PCI (cPCI) crates with 16-bit analog I/O to control instrumentation. To make the IP modules interchangeable, each module is calibrated for gain and offset compensation. We initially developed a method of verifying and calibrating the IP modules in a lab bench test environment using a PC with LabVIEW. The subsequent discovery that the ADCs have significant drift characteristics over periods of days of installed operation prompted development of an "in-situ" calibration process--one in which the IP modules can be calibrated without removing them from the cPCI crates in the storage ring. This paper discusses the original LabVIEW PC calibration and the migration to the proposed in-situ EPICS control system calibration.

      Cover page: In-situ calibration: migrating control system IP module calibration from the bench to the storage ring
      • Article
      • Peer Reviewed
      UCLA Previously Published Works (2021)
      Naturally occurring enzymes can be a source of unnatural reactivity that can be molded by directed evolution to generate efficient biocatalysts with valuable activities. Owing to the lack of exploitable stereocontrol elements in synthetic systems, steering the absolute and relative stereochemistry of free-radical processes is notoriously difficult in asymmetric catalysis. Inspired by the innate redox properties of first-row transition-metal cofactors, we repurposed cytochromes P450 to catalyze stereoselective atom-transfer radical cyclization. A set of metalloenzymes was engineered to impose substantial stereocontrol over the radical addition step and the halogen rebound step in these unnatural processes, allowing enantio- and diastereodivergent radical catalysis. This evolvable metalloenzyme platform represents a promising solution to tame fleeting radical intermediates for asymmetric catalysis.
        Cover page: Stereodivergent atom-transfer radical cyclization by engineered cytochromes P450
        • Article
        • Peer Reviewed
        UC Santa Barbara Previously Published Works (2024)
        The effective design of combinatorial libraries to balance fitness and diversity facilitates the engineering of useful enzyme functions, particularly those that are poorly characterized or unknown in biology. We introduce MODIFY, a machine learning (ML) algorithm that learns from natural protein sequences to infer evolutionarily plausible mutations and predict enzyme fitness. MODIFY co-optimizes predicted fitness and sequence diversity of starting libraries, prioritizing high-fitness variants while ensuring broad sequence coverage. In silico evaluation shows that MODIFY outperforms state-of-the-art unsupervised methods in zero-shot fitness prediction and enables ML-guided directed evolution with enhanced efficiency. Using MODIFY, we engineer generalist biocatalysts derived from a thermostable cytochrome c to achieve enantioselective C-B and C-Si bond formation via a new-to-nature carbene transfer mechanism, leading to biocatalysts six mutations away from previously developed enzymes while exhibiting superior or comparable activities. These results demonstrate MODIFY's potential in solving challenging enzyme engineering problems beyond the reach of classic directed evolution.
          Cover page: Machine learning-guided co-optimization of fitness and diversity facilitates combinatorial library design in enzyme engineering
          • Article
          Lawrence Berkeley National Laboratory (2001)
            Cover page: ALS superbend magnet performance
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