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Exam Number : ISSEP
Exam Name : Information Systems Security Engineering Professional
Vendor Name : ISC2
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ISSEP test Format | ISSEP Ctheirse Contents | ISSEP Ctheirse Outline | ISSEP test Syllabus | ISSEP test Objectives
Length of test
: 3 htheirs
Number of questions : 150
Question format : Multiple choice
Passing grade : 700 out of 1000 points
Exam availability : English
Testing center : Pearson VUE Testing Center
The Information Systems Security Engineering Professional (ISSEP) is a CISSP who specializes in the practical application of systems engineering principles and processes to develop secure systems. An ISSEP analyzes organizational needs, defines security requirements, designs security architectures, develops secure designs, implements system security, and supports system security test
and authorization for government and industry.
The broad spectrum of subjects
included in the ISSEP Common Body of Knowledge (CBK) ensure its relevancy across all disciplines in the field of security engineering. Successful candidates are competent in the following
5 domains:
• Security Engineering Principles
• Risk Management
• Security Planning, Design, and Implementation
• Secure Operations, Maintenance, and Disposal
• Systems Engineering Technical Management
Domains Theyight
1. Security Engineering Principles 22%
2. Risk Management 24%
3. Security Planning, Design, and Implementation 22%
4. Secure Operations, Maintenance, and Disposal 21%
5. Systems Engineering Technical Management 11%
Total: 100%
Domain 1:
Security Engineering Principles
1.1 General Security Principles
1.2 Security Risk Management Principles
1.3 System Resilience Principles
1.4 Vulnerability Management Principles
» Align security risk management with enterprise risk management
» Integrate risk management throughout the lifecycle
» Identify organizational security authority
» Identify elements of a system security policy
» Understand trust concepts and hierarchies
» Determine boundaries governed by security
policies
» Specify complete mediation
» Determine least common mechanism
» Understand open design concepts
» Analyze psychological acceptability/usability
» Understand the importance of consistent measurement
» Apply resilience methods to address threats
» Understand concepts of layered security
» Specify fail-safe defaults
» Avoid single points of failure
» Incorporate least privilege concepts
» Understand economy of mechanism
» Understand separation of privilege/duties concepts
» Understand security best practices applicable to the context
Domain 2:
Risk Management
2.1 Risk Management Process
2.2 Operational Risk Management
» Confirm operational risk appetite
» Identify remediation needs and other system changes
» Propose remediation for unaccepted security risks
» Assess proposed remediation or change activities
» Participate in implementation of the remediation or change
» Perform verification and validation activities relative to the requirements impacted
» Update risk test
documentation to account for the impact of the remediation or change
» Establish risk context
» Identify system security risks
» Perform risk analysis
» Perform risk evaluation
» Recommend risk treatment options
Domain 3:
Security Planning, Design, and Implementation
3.1 Stakeholder Requirements Definition
3.2 Requirements Analysis
3.3 System Security Architecture and Design
3.4 Implementation, Integration, and Deployment of Systems or System Modifications
3.5 Verification and Validation of Systems or System Modifications
Domain 3:
Security Planning, Design, and Implementation
» Define security roles and responsibilities
» Understand stakeholders mission/business and operational environment
» Identify security-relevant constraints and assumptions
» Identify and assess threats to assets
» Determine protection needs
» Document stakeholder requirements
» Analyze stakeholder requirements
» Develop system security context
» Identify security functions within the security concept of operations
» Develop system security requirements baseline
» Analyze and define security constraints
» Analyze system security requirements for completeness, adequacy, conflicts, and inconsistencies
» Perform functional analysis and allocation
» Maintain mutual traceability bettheyen specified design and system requirements
» Define system security design components
» Perform trade-off studies for system components
» Assess information protection effectiveness
Domain 4:
Secure Operations, Maintenance, and Disposal
4.1 Secure Operations
4.2 Secure Maintenance
4.3 Secure Disposal
» Document and maintain secure operations strategy
» Maintain and monitor continuous monitoring processes
» Support the incident response process
» Develop and direct secure maintenance strategy
» Participate in system remediation and change management processes
» Perform scheduled security reviews
» Develop and direct secure disposal strategy
» Verify proper security protections are in place during the decommissioning and disposal processes
» Document all actions and results of the disposal process
Domain 5:
Systems Engineering Technical Management
5.1 Acquisition Process
5.2 System Development Methodologies
5.3 Technical Management Processes
» Prepare security requirements for acquisitions
» Participate in vendor selection
» Participate in supply chain risk management
» Participate in contractual documentation development to verify security inclusion
» Perform acquisition acceptance verification and validation
» Integrate security tasks and activities into system development methodologies
» Verify security requirements are met throughout the process
» Identify opportunities for automation of security processes
» Perform project planning processes
» Perform project test
and control processes
» Perform decision management processes
» Perform risk management processes
» Perform configuration management processes
» Perform information management processes
» Perform measurement processes
» Perform quality assurance processes
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ISC2 Systems syllabus
Integrated Science Center (ISC)
ISC Operations Documents ISC Systems Documentation ISC2's Entry-Level Cyber Certification Wins Best Professional Certification AwardSC Media's 2023 Awards honor Certified in Cybersecurity℠ for its role in helping to close the global cyber workforce gap ALEXANDRIA, Va., Aug. 21, 2023 /PRNewswire/ -- ISC2 – the world's leading nonprofit member organization for cybersecurity professionals – today announced its entry-level certification Certified in Cybersecurity℠ (CC) has won a 2023 SC Award in the Excellence Award category for the Best Professional Certification Program. The Certified in Cybersecurity (CC) training and test was designed to address the global cyber workforce gap of 3.4 million professionals by providing a way for those from non-technical backgrounds to enter the field. The SC Awards program is cybersecurity's most prestigious and competitive program, recognizing the solutions, organizations and people driving innovation and success in information security. According to the SC Award's esteemed panel of independent judges, "ISC2's Certified in Cybersecurity certificate program is a cut above the rest," and it commended the program for its "contribution to the greater good of the cybersecurity community." The judges honored ISC2 for its "innovation, leadership and hard work." "This year's SC Award winners reflected their industry in flux," said Tom Spring, SC Media's Editorial Director at CyberRisk Alliance. "Winners demonstrated uncanny market agility and brought innovative solutions to help their customers stay ahead of increasingly sophisticated adversaries and emerging threats." "This award, along with the accomplishment of having over 28,000 individuals attain the Certified in Cybersecurity certification, underscores the value of this entry-level certification to their members and candidates who have diligently earned it, showcasing their unwavering commitment to the cybersecurity profession," said Clar Rosso, CEO, ISC2. "Recognition from SC Media's prestigious cybersecurity award program further validates the importance of their entry-level certification for the profession at large, as they attract new entrants into the field as organizations face acute staffing shortages. They're demonstrating that having a passion and drive to enter a career can open limitless opportunities for both professionals and employers." Diverse Pathways into the Cybersecurity Profession The CC℠ certification allows individuals from all backgrounds to demonstrate the foundational knowledge, skills and abilities for an entry- or junior-level cybersecurity role. The certification requires no prior work experience and can test a person's aptitude and interest in a cybersecurity career, allowing employers to confidently build resilient cyber teams across all experience levels. As part of ISC2's commitment to help close the workforce gap, its global initiative, One Million Certified in Cybersecurity, is offering free CC℠ training and exams to the first million people who enroll. Since its launch in August 2022, ISC2 has enrolled more than 250,000 individuals in the certification training, with more than 28,000 becoming certification holders. The global success of the certification highlights the importance of creating new and diverse pathways into the industry and removing barriers to entry into the profession. "I'm switching career paths to move into cybersecurity. Certified in Cybersecurity is a great way to demonstrate my knowledge," said Eric Turner, Cybersecurity Analyst, First Merchants Bank. This recognition follows ISC2's award win for the Best Professional Training or Certification Program at the 2023 SC Awards Europe. To learn more about the ISC2 Certified in Cybersecurity certification, please visit: https://www.isc2.org/Certifications/CC. About ISC2 ISC2 is the world's leading nonprofit member organization for cybersecurity professionals with an aim of inspiring a safe and secure cyber world. Best known for the acclaimed Certified Information Systems Security Professional (CISSP®) certification, ISC2 offers a portfolio of credentials that are part of a holistic, pragmatic approach to security. Their association of candidates, associates and members, more than 500,000 strong, is made up of certified cyber, information, software and infrastructure security professionals who are making a difference and helping to advance the industry. Their vision is supported by their commitment to educate and reach the general public through their charitable foundation – The Center for Cyber Safety and Education™. For more information on ISC2, visit www.isc2.org, follow us on X or connect with us on Facebook and LinkedIn. About CyberRisk Alliance CyberRisk Alliance (CRA) is a business intelligence company serving the high growth, rapidly evolving cybersecurity community with a diversified portfolio of services that inform, educate, build community, and inspire an efficient marketplace. Their trusted information leverages a unique network of jtheirnalists, analysts and influencers, policymakers, and practitioners. CRA's brands include SC Media, Security Theyekly, ChannelE2E, MSSP Alert, InfoSec World, Identiverse, Cybersecurity Collaboration Forum, its research unit CRA Business Intelligence, the peer-to-peer CISO membership network, Cybersecurity Collaborative, the Official Cyber Security Summit, TECHEXPO Top Secret, and now LaunchTech Communications. Click here to learn more. © 2023 ISC2 Inc., ISC2, CISSP, SSCP, CCSP, CGRC, CSSLP, HCISPP, CISSP-ISSAP, CISSP-ISSEP, CISSP-ISSMP and CBK are registered marks, and CC is a service mark of ISC2, Inc. Media Contact:Amanda Steinman Senior PR Manager ISC2 asteinman@isc2.org View original content:https://www.prnewswire.com/news-releases/isc2s-entry-level-cyber-certification-wins-best-professional-certification-award-301904977.htmlSTHEIRCE ISC2 © 2023 Benzinga.com. Benzinga does not provide investment advice. All rights reserved. Building Fe–S proteins: bacterial strategiesBeinert, H. Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5, 2–15 (2000). A review from a pioneer in the Fe–S protein field. Fontecave, M. Iron-sulfur clusters: ever-expanding roles. Nature Chem. Biol. 2, 171–174 (2006). Kiley, P. J. & Beinert, H. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol. 6, 181–185 (2003). Ayala-Castro, C., Saini, A. & Outten, F. W. Fe-S cluster assembly pathways in bacteria. Microbiol. Mol. Biol. Rev. 72, 110–125 (2008). Fontecave, M., Py, B., Ollagnier de Choudens, S. & Barras, F. 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Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference bettheyen L-cysteine desulfurase and L-selenocysteine lyase reactions. J. Biochem. 127, 559–567 (2000). Schwartz, C. J., Djaman, O., Imlay, J. A. & Kiley, P. J. The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc. Natl Acad. Sci. USA 97, 9009–9014 (2000). Mueller, E. G. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nature Chem. Biol. 2, 185–194 (2006). Ikeuchi, Y., Shigi, N., Kato, J., Nishimura, A. & Suzuki, T. Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thitheiridine biosynthesis at tRNA wobble positions. Mol. Cell 21, 97–108 (2006). Nilsson, K, Lundgren, H. K., Hagervall, T. G. & Björk, G. R. The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium. J. 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Tokumoto, U., Kitamura, S., Fukuyama, K. & Takahashi, Y. Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J. Biochem. 136, 199–209 (2004). Loiseau, L. et. al. Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J. Biol. Chem. 280, 26760–26769 (2005). Trotter, V. et al. The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol. Microbiol. 74, 1527–1542 (2009). Urbina, H. D., Silberg, J. J., Hoff, K. G. & Vickery, L. E. Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. J. Biol. Chem. 276, 44521–44526 (2001). Smith, A. D. et al. Sulfur transfer from IscS to IscU: the first step in iron-sulfur cluster biosynthesis. J. Am. Chem. Soc. 123, 11103–11104 (2001). Loiseau, L., Ollagnier de Choudens, S., Nachin, L., Fontecave, M. & Barras, F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J. Biol. Chem. 278, 38352–38359 (2003). Ollagnier de Choudens, S. et al. Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE. FEBS Lett. 555, 263–267 (2003). Outten, F. W., Wood, M. J., Munoz, F. M. & Storz, G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J. Biol. Chem. 278, 45713–45719 (2003). Layer, G. et al.SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly. J. Biol. Chem. 282, 13342–13350 (2007). The first evidence for the identification of SufBCD as the scaffold in the Suf system. Sendra, M., Ollagnier de Choudens, S., Lascoux, D., Sanakis, Y. & Fontecave, M. The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett. 581, 1362–1368 (2007). Layer, G., Ollagnier de Choudens, S., Sanakis, Y. & Fontecave, M. Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J. Biol. Chem. 281, 16256–16263 (2006). Adinolfi, S. et al. Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS. Nature Struct. Mol. Biol. 16, 390–396 (2009). Shi, R. et al. Structural basis for Fe–S cluster assembly and tRNA thiolation mediated by IscS protein–protein interactions. PLoS Biol. 8, e1000354 (2010). Pandolfo, M. & Pastore, A. The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J. 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Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 155, 295–304 (2009). Ding, H. & Clark, R. J. Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem. J. 379, 433–440 (2004). Ding, H., Harrison, K. & Lu, J. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J. Biol. Chem. 280, 30432–30437 (2005). Yang, J., Bitoun, J. P. & Ding, H. Interplay of IscA and IscU in biogenesis of iron-sulfur clusters. J. Biol. Chem. 281, 27956–27963 (2006). Lu, J., Yang, J., Tan, G. & Ding, H. Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli. Biochem. J. 409, 535–543 (2008). Djaman, O., Outten, F. W. & Imlay, J. A. Repair of oxidized iron-sulfur clusters in Escherichia coli. J. Biol. Chem. 279, 44590–44599 (2004). 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Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: implications for the mechanism of iron-sulfur cluster assembly. Proc. Natl Acad. Sci. USA 99, 5948–5952 (2002). Unciuleac, M. C. et al. In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry 46, 6812–6821 (2007). Shimomura, Y., Wada, K., Fukuyama, K. & Takahashi, Y. The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis. J. Mol. Biol. 383, 133–143 (2008). Vickery, L. E. & Cupp-Vickery, J. R. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit. Rev. Biochem. Mol. Biol. 42, 95–111 (2007). An account of the studies of co-chaperones in Fe–Scluster biogenesis by prominent contributors in the field. Chandramouli, K. & Johnson, M. K. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 45, 11087–11095 (2006). Bonomi, F., Iametti, S., Morleo, A., Ta, D. & Vickery, L. E. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Biochemistry 47, 12795–12801 (2008). Petrovic, A. et al. Hydrodynamic characterization of the SufBC and SufCD complexes and their interaction with fluorescent adenosine nucleotides. Protein Sci. 17, 1264–1274 (2008). Wada, K. et al. Molecular dynamism of Fe-S cluster biosynthesis implicated by the structure of the SufC2-SufD2 complex. J. Mol. Biol. 387, 245–258 (2009). Chahal, H. K, Dai, Y., Saini, A., Ayala-Castro, C. & Outten, F. W. The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer. Biochemistry 48, 10644–10653 (2009). Eccleston, J. F., Petrovic, A., Davis, C. T., Rangachari, K. & Wilson, R. J. The kinetic mechanism of the SufC ATPase: the cleavage step is accelerated by SufB. J. Biol. Chem. 281, 8371–8378 (2006). Vinella, D., Brochier-Armanet, C., Loiseau, L., Talla, E. & Barras, F. Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet. 5, e1000497 (2009). An in vivo analysis of the specificities and redundancies of A-type proteins. Krebs, C. et al. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry 40, 14069–14680 (2001). Ollagnier de Choudens, S. et al. SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly. J. Biol. Chem. 278, 17993–18001 (2003). Loiseau, L. et al. ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc. Natl Acad. Sci. USA 104, 13626–13631 (2007). This paper reports the first case of in vivo specificity bettheyen an A-type protein and a target apoprotein. Gupta, V. et al. Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J. Am. Chem. Soc. 131, 6149–6153 (2009). A demonstration that, in vivo , IscA binds to Fe–S clusters. Zeng, J. et al. The IscA from Acidithiobacillus ferrooxidans is an iron-sulfur protein, which assembles the [4Fe-4S] cluster with intracellular iron and sulfur. Arch. Biochem. Biophys. 463, 237–244 (2007). Ollagnier de Choudens, S., Sanakis, Y. & Fontecave, M. SufA/IscA: reactivity studies of a class of scaffold proteins involved in [Fe-S] cluster assembly. J. Biol. Inorg. Chem. 9, 828–838 (2004). Mettert, E. L., Outten, F. W., Wanta, B. & Kiley, P. J. The impact of O2 on the Fe-S. cluster biogenesis requirements of Escherichia coli FNR. J. Mol. Biol. 384, 798–811 (2008). Tan, G., Lu, J., Bitoun, J. P., Huang, H. & Ding, H. IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions. Biochem. J. 420, 463–472 (2009). Angelini, S. et al. NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions. J. Biol. Chem. 283, 14084–14091 (2008). Bandyopadhyay, S. et al. A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier. J. Biol. Chem. 283, 14092–14099 (2008). Balasubramanian, R., Shen, G., Bryant, D. A. & Golbeck, J. H. Regulatory roles for IscA and SufA in iron homeostasis and redox stress responses in the cyanobacterium Synechococcus sp. strain PCC 7002. J. Bacteriol. 188, 3182–3191 (2006). Jin, Z. et al. Biogenesis of iron-sulfur clusters in photosystem I: holo-NfuA from the cyanobacterium Synechococcus sp. PCC 7002 rapidly and efficiently transfers [4Fe-4S] clusters to apo-PsaC in vitro. J. Biol. Chem. 283, 28426–28435 (2008). Agar, J. N. et al. Modular organization and identification of a mononuclear iron-binding site within the NifU protein. J. Biol. Inorg. Chem. 5, 167–177 (2000). Boyd, J. M., Sondelski, J. L. & Downs, D. M. Bacterial ApbC protein has two biochemical activities that are required for in vivo function. J. Biol. Chem. 284, 110–118 (2009). An important contribution to the understanding of the role of one of the most conserved proteins in all living organisms. Boyd, J. M., Pierik, A. J., Netz, D. J., Lill, R. & Downs, D. M. Bacterial ApbC can bind and effectively transfer iron-sulfur clusters. Biochemistry 47, 8195–81202 (2008). Boyd, J. M., Lewis, J. A., Escalante-Semerena, J. C. & Downs, D. M. Salmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy bettheyen ApbC and IscU. J. Bacteriol. 190, 4596–4602 (2008). Bych, K. et al. The iron-sulphur protein Ind1 is required for effective complex I assembly. EMBO J. 27, 1736–1746 (2008). An example of the use of in vivo labelling to elucidate the position of an Fe–S cluster biogenesis factor in a pathway. Justino, M. C., Baptista, J. M. & Saraiva, L. M. Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair. Biometals 22, 99–108 (2009). Overton, T. W. et al. Widespread distribution in pathogenic bacteria of di-iron proteins that repair oxidative and nitrosative damage to iron-sulfur centers. J. Bacteriol. 190, 2004–2013 (2008). Harrington, J. C. et al. Resistance of Haemophilus influenzae to reactive nitrogen donors and gamma interferon-stimulated macrophages requires the formate-dependent nitrite reductase regulator-activated ytfE gene. Infect. Immun. 77, 1945–1958 (2009). Vine, C. E., Justino, M. C., Saraiva, L. M. & Cole, J. 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Protection from superoxide damage associated with an increased level of the YggX protein in Salmonella enterica. Proc. Natl Acad. Sci. USA 98, 8030–8035 (2001). Tucker, N. P. et al. The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster. PLoS ONE 3, e3623 (2008). Schwartz, C. J. et al. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl Acad. Sci. USA 98, 14895–14900 (2001). The proposal that an autoregulatory system allows bacterial cells to sense Fe–S cluster homeostasis. Giel, J. L., Rodionov, D., Liu, M., Blattner, F. R. & Kiley, P. J. IscR-dependent gene expression links iron-sulphur cluster assembly to the control of O2-regulated genes in Escherichia coli. Mol. Microbiol. 60, 1058–1075 (2006). This paper shows that IscR regulates a broad range of genes. Wu, Y. & Outten, F. W. 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Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA. EMBO J. 28, 1551–1561 (2009). The first example of a role for small-RNA-mediated regulation in Fe–S cluster homeostasis. |
The Integrated Science Center (ISC) sits next to Lemon and Hardy Residence Halls on Barksdale Field. The facility was constructed to integrate William & Mary’s science programs; allowing increased opportunity for multidisciplinary research. Currently, the ISC is the only place on campus where ctheirses and research projects in Applied Science, Biology, Chemistry, Neuroscience, Physics and Psychology exists in the same building. With over 100,000 sq. ft. of space, the ISC consists of a large seminar room, colloquiums, teaching and research labs, a machine shop, glass-blowing faculty, instrument rooms, reading rooms and eat-in kitchens. Research laboratories are equipped with various levels of fume hoods, biosafety cabinets, laboratory equipment, computing equipment, and laboratory emergency equipment including eyewashes, spill kits and fire extinguishers. On the campus of William & Mary, this is the only building with biological and hazardous waste accumulation rooms managed by the EH&S Office.
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